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Q60929

- MEF2A_MOUSE

UniProt

Q60929 - MEF2A_MOUSE

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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

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 kinase binding 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: MGI
  10. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  11. RNA polymerase II transcription coactivator activity Source: Ensembl
  12. sequence-specific DNA binding Source: MGI
  13. sequence-specific DNA binding transcription factor activity Source: MGI
  14. 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. transcription from RNA polymerase II promoter Source: GOC
  14. ventricular cardiac myofibril assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_215063. ERK/MAPK targets.
REACT_258600. CDO in myogenesis.

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. cytoplasm Source: Ensembl
  2. nuclear chromatin Source: BHF-UCL
  3. nucleus Source: UniProtKB
Complete GO annotation...

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

MaxQBiQ60929.
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

BgeeiQ60929.
CleanExiMM_MEF2A.
ExpressionAtlasiQ60929. baseline and differential.
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

        10         20         30         40         50
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS
60 70 80 90 100
SNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD
110 120 130 140 150
ADDYFEHSPL SEDRFSKLNE DSDFIFKRGP PGLPPQNFSM SVTVPVTSPN
160 170 180 190 200
ALSYTNPGSS LVSPSLAASS TLADSSMLSP PPATLHRNVS PGAPQRPPST
210 220 230 240 250
GSASGMLSTT DLTVPNGAGN SPVGNGFVNS RASPNLIGNT GANSLGKVMP
260 270 280 290 300
TKSPPPPGGG SLGMNSRKPD LRVVIPPSSK GMMPPLSEEE ELELNAQRIS
310 320 330 340 350
SSQATQPLAT PVVSVTTPSL PPQGLVYSAM PTAYNTDYSL TSADLSALQG
360 370 380 390 400
FTSPGMLSLG QASAWQQHHL GQAALSSLVA GGQLSQGSNL SINTNQNINI
410 420 430 440 450
KSEPISPPRD RMTPSGFQQQ QQQPQQQPPP QPPQPQPRQE MGRSPVDSLS
460 470 480 490
SSSSSYDGSD REDPRGDFHS PIVLGRPPNT EDRESPSVKR MRMDTWVT
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

MaxQBi Q60929.
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.
REACT_258600. CDO in myogenesis.

Miscellaneous databases

ChiTaRSi Mef2a. mouse.
NextBioi 291742.
PROi Q60929.
SOURCEi Search...

Gene expression databases

Bgeei Q60929.
CleanExi MM_MEF2A.
ExpressionAtlasi Q60929. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 128 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