Myocyte-specific enhancer factor 2A

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Reviewed, UniProtKB/Swiss-Prot Q02078 (MEF2A_HUMAN)

Last modified July 7, 2009. Version 92. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Myocyte-specific enhancer factor 2A
Alternative name(s):
Serum response factor-like protein 1

Gene names

Name:	MEF2A
Synonyms:	MEF2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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. Ref.8 Ref.11 Ref.13 Ref.15 Ref.18 Ref.19 Ref.20
Subunit structure	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.
Subcellular location	Nucleus. Ref.13 Ref.18
Tissue specificity	Isoform MEF2 and isoform MEFA are expressed only in skeletal and cardiac muscle and in the brain while isoform RSRFC4 and isoform RSRFC9 are expressed in all tissues examined. Ref.1 Ref.3
Post-translational modification	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 transciptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF. Ref.8 Ref.13 Ref.19 Ref.20 Ref.6 Ref.9 Ref.10 Ref.12 Ref.16 Ref.21 Ref.23 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 by SUMO1 and, to a lesser extent by SUMO2 and SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites in the cerebellar cortex and promotes their morphogenesis 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. 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. Ref.8 Ref.13 Ref.19 Ref.20 Ref.6 Ref.9 Ref.10 Ref.12 Ref.16 Ref.21 Ref.23
Involvement in disease	Defects in MEF2A might be a cause of autosomal dominant coronary artery disease 1 with myocardial infarction (ADCAD1) [MIM:608320].
Sequence similarities	Belongs to the MEF2 family. Contains 1 MADS-box domain. Contains 1 Mef2-type DNA-binding domain.

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Ontologies

Keywords
Biological process	Apoptosis Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW muscle organ development Ref.3 Traceable author statement. Source: ProtInc nervous system development Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.3 Traceable author statement. Source: ProtInc
Molecular function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro transcription factor activity Non-traceable author statement. Source: ProtInc
Complete GO annotation...

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Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform MEF2 (identifier: Q02078-1) 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.

Isoform MEFA (identifier: Q02078-2) The sequence of this isoform differs from the canonical sequence as follows: 87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP

Isoform RSRFC4 (identifier: Q02078-3) The sequence of this isoform differs from the canonical sequence as follows: 289-296: Missing. 420-421: Missing.

Isoform RSRFC9 (identifier: Q02078-4) The sequence of this isoform differs from the canonical sequence as follows: 87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP 289-296: Missing. 420-421: Missing.

Isoform 5 (identifier: Q02078-5) The sequence of this isoform differs from the canonical sequence as follows: 289-296: Missing.
Note: No experimental confirmation available.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 507

507

Myocyte-specific enhancer factor 2A

PRO_0000199428

Regions

Domain

3 – 57

MADS-box

DNA binding

58 – 86

Mef2-type Potential

Region

266 – 283

Required for interaction with MAPKs

Region

289 – 296

Beta domain

Compositional bias

4 – 31

Lys-rich (basic)

Compositional bias

141 – 186

Ser/Thr-rich

Compositional bias

420 – 446

Gln/Pro-rich

Sites

Site

176 – 177

Cleavage Probable

Site

213 – 214

Cleavage Probable

Site

466 – 467

Cleavage Probable

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphoserine; by CK2 By similarity

Modified residue

Phosphoserine By similarity

Modified residue

108

Phosphothreonine By similarity

Modified residue

114

N6-acetyllysine By similarity

Modified residue

117

N6-acetyllysine By similarity

Modified residue

235

Phosphoserine Ref.23

Modified residue

249

N6-acetyllysine By similarity

Modified residue

254

N6-acetyllysine By similarity

Modified residue

255

Phosphoserine; by MAPK14 Ref.12 Ref.23

Modified residue

270

N6-acetyllysine By similarity

Modified residue

282

N6-acetyllysine By similarity

Modified residue

312

Phosphothreonine; by MAPK7 and MAPK14 Ref.8 Ref.9 Ref.10 Ref.12 Ref.21

Modified residue

312

Phosphothreonine; by NLK Ref.8 Ref.9 Ref.10 Ref.12 Ref.21

Modified residue

319

Phosphothreonine; by MAPK7 and MAPK14 Ref.8 Ref.9 Ref.10 Ref.12

Modified residue

355

Phosphoserine; by MAPK7 Ref.10

Modified residue

403

N6-acetyllysine; alternate By similarity

Modified residue

408

Phosphoserine; by CDK5 Ref.13 Ref.19 Ref.20 Ref.12

Modified residue

453

Phosphoserine; by MAPK Ref.8

Cross-link

403

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.18 Ref.19

Natural variations

Alternative sequence

87 – 132

ALNKK…NHKIA → TLRKKGLNGCESPDADDYFE HSPLSEDRFSKLNEDSDFIF KRGP in isoform MEFA and isoform RSRFC9.

VSP_006240

Alternative sequence

289 – 296

Missing in isoform RSRFC4, isoform RSRFC9 and isoform 5.

VSP_006241

Alternative sequence

420 – 421

Missing in isoform RSRFC4 and isoform RSRFC9.

VSP_006242

Natural variant

263

N → S Ref.24

VAR_038407

Natural variant

279

P → L Ref.24 Ref.25 Ref.26

VAR_038408

Natural variant

283

G → D Ref.24

VAR_038409

Natural variant

440 – 446

Missing Loss of nuclear localization; 66% decrease in transcription activation; loss of synergistic activation by MEF2A and GATA1 through a dominant-negative mechanism.

VAR_017743

Experimental info

Mutagenesis

176

D → A: Abolishes cleavage at sites 1 and 2 by caspase 3. Increased cleavage at site 3 by caspase 3. Ref.11

Mutagenesis

213

D → A: Abolishes cleavage at sites 2 and 3 by caspase 7. Ref.11

Mutagenesis

255

S → A: Slightly increased MEF2A protein level. Ref.12

Mutagenesis

255

S → D: Decreased MEF2A protein level. Ref.12

Mutagenesis

269

R → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-270. Ref.9

Mutagenesis

270

K → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-269. Ref.9

Mutagenesis

273

L → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-275. Ref.9

Mutagenesis

275

V → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-273. Ref.9

Mutagenesis

277

I → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-278. Ref.9

Mutagenesis

278

P → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-277. Ref.9

Mutagenesis

312

T → A: Greatly reduced p38-mediated phosphorylation. Abolishes p38-mediated transcriptional activation; when associated with A-319. Ref.8 Ref.10

Mutagenesis

319

T → A: Greatly reduced p38-mediated phosphorylation. Abolishes P38-mediated transcriptional activation; when associated with A-312. Ref.8 Ref.10

Mutagenesis

355

S → A: No effect on p38-mediated transcriptional avtivity. Ref.8 Ref.10

Mutagenesis

387

S → A: No effect on p38-mediated phosphorylation.

Mutagenesis

403

K → R: Abolishes sumoylation. No change in subcellular location nor in DNA binding. Loss of transcriptional repression. Ref.18 Ref.19

Mutagenesis

408

S → A: Loss of sumoylation. Ref.13 Ref.19

Mutagenesis

408

S → D: Rescues sumoylation. Ref.13 Ref.19

Mutagenesis

453

S → A: No effect on p38-mediated phosphorylation. Ref.8

Mutagenesis

479

S → A: No effect on p38-mediated phosphorylation. Ref.8

Sequence conflict

430

Missing in AAB17195. Ref.4

Sequence conflict

430

Missing in AAB17196. Ref.4

Secondary structure

507

Helix Strand Turn

Details...

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Sequences

Sequence		Length	Mass (Da)
Isoform MEF2 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 362BA4FBCC792CE2 Show »	FASTA	507	54,811
10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD PDTSYVLTPH TEEKYKKINE 130 140 150 160 170 180 EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS PNALSYTNPG SSLVSPSLAA SSTLTDSSML 190 200 210 220 230 240 SPPQTTLHRN VSPGAPQRPP STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG 250 260 270 280 290 300 ATGANSLGKV MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLSE EEELELNTQR 310 320 330 340 350 360 ISSSQATQPL ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL QGFNSPGMLS 370 380 390 400 410 420 LGQVSAWQQH HLGQAALSSL VAGGQLSQGS NLSINTNQNI SIKSEPISPP RDRMTPSGFQ 430 440 450 460 470 480 QQQQQQQQQQ PPPPPQPQPQ PPQPQPRQEM GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP 490 500 IVLGRPPNTE DRESPSVKRM RMDAWVT « Hide
Isoform MEFA. Checksum: E0032FA6F955D7F7 Show »	FASTA	505	54,442
10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD ADDYFEHSPL SEDRFSKLNE 130 140 150 160 170 180 DSDFIFKRGP PGLPPQNFSM SVTVPVTSPN ALSYTNPGSS LVSPSLAASS TLTDSSMLSP 190 200 210 220 230 240 PQTTLHRNVS PGAPQRPPST GNAGGMLSTT DLTVPNGAGS SPVGNGFVNS RASPNLIGAT 250 260 270 280 290 300 GANSLGKVMP TKSPPPPGGG NLGMNSRKPD LRVVIPPSSK GMMPPLSEEE ELELNTQRIS 310 320 330 340 350 360 SSQATQPLAT PVVSVTTPSL PPQGLVYSAM PTAYNTDYSL TSADLSALQG FNSPGMLSLG 370 380 390 400 410 420 QVSAWQQHHL GQAALSSLVA GGQLSQGSNL SINTNQNISI KSEPISPPRD RMTPSGFQQQ 430 440 450 460 470 480 QQQQQQQQPP PPPQPQPQPP QPQPRQEMGR SPVDSLSSSS SSYDGSDRED PRGDFHSPIV 490 500 LGRPPNTEDR ESPSVKRMRM DAWVT « Hide
Isoform RSRFC4. Checksum: A255A8EDC8B07FB0 Show »	FASTA	497	53,596
10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD PDTSYVLTPH TEEKYKKINE 130 140 150 160 170 180 EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS PNALSYTNPG SSLVSPSLAA SSTLTDSSML 190 200 210 220 230 240 SPPQTTLHRN VSPGAPQRPP STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG 250 260 270 280 290 300 ATGANSLGKV MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLNT QRISSSQATQ 310 320 330 340 350 360 PLATPVVSVT TPSLPPQGLV YSAMPTAYNT DYSLTSADLS ALQGFNSPGM LSLGQVSAWQ 370 380 390 400 410 420 QHHLGQAALS SLVAGGQLSQ GSNLSINTNQ NISIKSEPIS PPRDRMTPSG FQQQQQQQQQ 430 440 450 460 470 480 PPPPPQPQPQ PPQPQPRQEM GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP IVLGRPPNTE 490 DRESPSVKRM RMDAWVT « Hide
Isoform RSRFC9. Checksum: 3C083C4EFC3872F0 Show »	FASTA	495	53,227
10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD ADDYFEHSPL SEDRFSKLNE 130 140 150 160 170 180 DSDFIFKRGP PGLPPQNFSM SVTVPVTSPN ALSYTNPGSS LVSPSLAASS TLTDSSMLSP 190 200 210 220 230 240 PQTTLHRNVS PGAPQRPPST GNAGGMLSTT DLTVPNGAGS SPVGNGFVNS RASPNLIGAT 250 260 270 280 290 300 GANSLGKVMP TKSPPPPGGG NLGMNSRKPD LRVVIPPSSK GMMPPLNTQR ISSSQATQPL 310 320 330 340 350 360 ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL QGFNSPGMLS LGQVSAWQQH 370 380 390 400 410 420 HLGQAALSSL VAGGQLSQGS NLSINTNQNI SIKSEPISPP RDRMTPSGFQ QQQQQQQQPP 430 440 450 460 470 480 PPPQPQPQPP QPQPRQEMGR SPVDSLSSSS SSYDGSDRED PRGDFHSPIV LGRPPNTEDR 490 ESPSVKRMRM DAWVT « Hide
Isoform 5. Checksum: FE3A83DDCE477C27 Show »	FASTA	499	53,852
10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD PDTSYVLTPH TEEKYKKINE 130 140 150 160 170 180 EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS PNALSYTNPG SSLVSPSLAA SSTLTDSSML 190 200 210 220 230 240 SPPQTTLHRN VSPGAPQRPP STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG 250 260 270 280 290 300 ATGANSLGKV MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLNT QRISSSQATQ 310 320 330 340 350 360 PLATPVVSVT TPSLPPQGLV YSAMPTAYNT DYSLTSADLS ALQGFNSPGM LSLGQVSAWQ 370 380 390 400 410 420 QHHLGQAALS SLVAGGQLSQ GSNLSINTNQ NISIKSEPIS PPRDRMTPSG FQQQQQQQQQ 430 440 450 460 470 480 QQPPPPPQPQ PQPPQPQPRQ EMGRSPVDSL SSSSSSYDGS DREDPRGDFH SPIVLGRPPN 490 TEDRESPSVK RMRMDAWVT « Hide

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References

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[1]	"Human SRF-related proteins: DNA-binding properties and potential regulatory targets." Pollock R., Treisman R. Genes Dev. 5:2327-2341(1991) [PubMed: 1748287] [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 RSFRC9), 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: 1516833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MEF2 AND RSFRC9), 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 RSFRC9).
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Tissue: Pancreas.
[6]	"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: 9753748] [Abstract] Cited for: INTERACTION WITH MAPK7, PHOSPHORYLATION.
[7]	"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: 10487761] [Abstract] Cited for: INTERACTION WITH HDAC4 AND HDAC9.
[8]	"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: 9858528] [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.
[9]	"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: 10330143] [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.
[10]	"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: 10849446] [Abstract] Cited for: PHOSPHORYLATION AT THR-312; THR-319 AND SER-355, MUTAGENESIS OF THR-312; THR-319 AND SER-355.
[11]	"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: 11904443] [Abstract] Cited for: PROTEOLYTIC PROCESSING AT ASP-176; ASP-213 AND ASP-466, FUNCTION, MUTAGENESIS OF ASP-176 AND ASP-213.
[12]	"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: 12586839] [Abstract] Cited for: PHOSPHORYLATION AT SER-255; THR-312; THR-319 AND SER-408, MASS SPECTROMETRY, MUTAGENESIS OF SER-255.
[13]	"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: 12691662] [Abstract] Cited for: PHOSPHORYLATION AT SER-408, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-408.
[14]	"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: 14630949] [Abstract] Cited for: INTERACTION WITH SLC2A4RG.
[15]	"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: 15834131] [Abstract] Cited for: FUNCTION OF BETA DOMAIN.
[16]	"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: 15888658] [Abstract] Cited for: PROTEOLYTIC PROCESSING, PHOSPHORYLATION.
[17]	"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: 15831463] [Abstract] Cited for: ACETYLATION.
[18]	"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: 16563226] [Abstract] Cited for: SUMOYLATION AT LYS-403, INTERACTION WITH PIAS1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-403.
[19]	"PDSM, a motif for phosphorylation-dependent SUMO modification." Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J., Nakai A., Sistonen L. Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006) [PubMed: 16371476] [Abstract] Cited for: SUMOYLATION AT LYS-403, PHOSPHORYLATION AT SER-408, FUNCTION, MUTAGENESIS OF LYS-403 AND SER-408.
[20]	"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: 16484498] [Abstract] Cited for: PHOSPHORYLATION AT SER-408, FUNCTION.
[21]	"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: 17785444] [Abstract] Cited for: PHOSPHORYLATION AT THR-312 BY NLK.
[22]	"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: 18697823] [Abstract] Cited for: ACETYLATION, CARDIAC HYPERTROPHY.
[23]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-255, MASS SPECTROMETRY.
[24]	"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: 15496429] [Abstract] Cited for: VARIANTS SER-263; LEU-279 AND ASP-283, CHARACTERISTICS OF VARIANTS SER-263; LEU-279 AND ASP-283.
[25]	"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: 15958500] [Abstract] Cited for: VARIANT LEU-279, ASSOCIATION WITH SUSCEPTIBILITY TO MYOCARDIAL INFARCTION.
[26]	"Lack of association between the MEF2A gene and myocardial infarction." Lieb W., Mayer B., Koenig I.R., Borwitzky I., Goetz A., Kain S., Hengstenberg C., Linsel-Nitschke P., Fischer M., Doering A., Wichmann H.E., Meitinger T., Kreutz R., Ziegler A., Schunkert H., Erdmann J. Circulation 117:185-191(2008) [PubMed: 18086930] [Abstract] Cited for: VARIANT LEU-279, LACK OF ASSOCIATION WITH MYOCARDIAL INFARCTION.
[27]	"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: 10835359] [Abstract] Cited for: STRUCTURE BY NMR OF 2-86 IN COMPLEX WITH DNA.
[28]	"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: 10715212] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-78 IN COMPLEX WITH DNA, DIMERIZATION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

Y16312 mRNA. Translation: CAA76175.1.
X63381 mRNA. Translation: CAA44979.1.
X68503 mRNA. Translation: CAA48516.1.
X68505 mRNA. Translation: CAA48517.1.
U49020

U49019 Genomic DNA. Translation: AAB17195.1.
U49020

U49019 Genomic DNA. Translation: AAB17196.1.
BC013437 mRNA. Translation: AAH13437.1.

IPI

IPI00219254.
IPI00219255.
IPI00398406.
IPI00555797.
IPI00747318.

PIR

C39481.
S25831.

RefSeq

NP_001124398.1.
NP_001124400.1.
NP_005578.2.

UniGene

Hs.268675

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C7U	NMR	-	A/B	2-86	[»]
1EGW	X-ray	1.50	A/B/C/D	2-78	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q02078.

Proteomic databases

PRIDE

Q02078.

Genome annotation databases

Ensembl

ENSG00000068305. Homo sapiens. [Contig view]

GeneID

4205.

KEGG

hsa:4205.

UCSC

uc002bve.1. human.
uc002bvf.1. human.
uc002bvh.2. human.

Organism-specific databases

GeneCards

GC15P097923.

H-InvDB

HIX0012611.

HGNC

HGNC:6993. MEF2A.

HPA

CAB004499.

MIM

600660. gene.
608320. phenotype.

PharmGKB

PA30731.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q02078.

HOVERGEN

Q02078.

Enzyme and pathway databases

Pathway_Interaction_DB

p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_11061. Signalling by NGF.

Gene expression databases

ArrayExpress

Q02078.

Bgee

Q02078.

CleanEx

HS_MEF2A.

GermOnline

ENSG00000068305. Homo sapiens.

Family and domain databases

InterPro

IPR002100. TF_MADSbox.
[Graphical view]

Pfam

PF00319. SRF-TF. 1 hit.
[Graphical view]

PRINTS

PR00404. MADSDOMAIN.

SMART

SM00432. MADS. 1 hit.
[Graphical view]

PROSITE

PS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

16568.

PMAP-CutDB

Q02078.

SOURCE

Search...

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Entry information

Entry name

MEF2A_HUMAN

Accession

Primary (citable) accession number: Q02078
Secondary accession number(s): O43814

Q96D14

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	July 7, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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