Q60929 (MEF2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myocyte-specific enhancer factor 2A

Gene names

Name:

Mef2a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 By similarity.
Subunit structure	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. Ref.4 Ref.6
Subcellular location	Nucleus.
Tissue specificity	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. Ref.1 Ref.5
Developmental stage	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. Ref.1
Domain	The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity By similarity.
Post-translational modification	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. Ref.6 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. 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. 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. Ref.6
Sequence similarities	Belongs to the MEF2 family. Contains 1 MADS-box domain. Contains 1 Mef2-type DNA-binding domain.

Ontologies

Keywords
Biological process	Apoptosis Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ERK5 cascade Inferred from sequence or structural similarity. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cardiac conduction Inferred from mutant phenotype PubMed 12379849. Source: UniProtKB cellular response to calcium ion Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial genome maintenance Inferred from mutant phenotype PubMed 12379849. Source: UniProtKB mitochondrion distribution Inferred from mutant phenotype PubMed 12379849. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW ventricular cardiac myofibril development Inferred from mutant phenotype PubMed 12379849. Source: UniProtKB
Cellular_component	nuclear chromatin Inferred from direct assay PubMed 20833138. Source: BHF-UCL
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay PubMed 16407236. Source: MGI RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 21379568. Source: MGI RNA polymerase II regulatory region sequence-specific DNA binding Inferred from sequence or structural similarity. Source: UniProtKB RNA polymerase II transcription coactivator activity Inferred from electronic annotation. Source: Compara SMAD binding Inferred from sequence or structural similarity. Source: UniProtKB chromatin binding Inferred from direct assay PubMed 16407236PubMed 18198354PubMed 21379568. Source: MGI histone acetyltransferase binding Inferred from sequence or structural similarity. Source: UniProtKB histone deacetylase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Nfix	P70257-2	2	EBI-2639094,EBI-2639084

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q60929-1)

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 2 (identifier: Q60929-2)

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

Isoform 3 (identifier: Q60929-3)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 498	498	Myocyte-specific enhancer factor 2A		PRO_0000199429
Regions
	Domain	3 – 57	55	MADS-box
	DNA binding	58 – 86	29	Mef2-type Potential
	Region	264 – 281	18	Required for interaction with MAPKs By similarity
	Region	287 – 294	8	Beta domain By similarity
	Compositional bias	254 – 257	4	Poly-Pro
	Compositional bias	288 – 293	6	Poly-Glu
	Compositional bias	418 – 439	22	Gln/Pro-rich
	Compositional bias	448 – 455	8	Poly-Ser
Sites
	Site	174 – 175	2	Cleavage Probable
	Site	211 – 212	2	Cleavage Probable
	Site	457 – 458	2	Cleavage Probable
Amino acid modifications
	Modified residue	59	1	Phosphoserine; by CK2 By similarity
	Modified residue	98	1	Phosphoserine Ref.7
	Modified residue	233	1	Phosphoserine By similarity
	Modified residue	247	1	N6-acetyllysine By similarity
	Modified residue	253	1	Phosphoserine By similarity
	Modified residue	310	1	Phosphothreonine; by MAPK7; alternate By similarity
	Modified residue	310	1	Phosphothreonine; by NLK; alternate Ref.6
	Modified residue	317	1	Phosphothreonine; by MAPK7 By similarity
	Modified residue	353	1	Phosphoserine; by MAPK7 By similarity
	Modified residue	401	1	N6-acetyllysine; alternate By similarity
	Modified residue	406	1	Phosphoserine By similarity
	Modified residue	444	1	Phosphoserine By similarity
	Cross-link	401		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Natural variations
	Alternative sequence	87 – 130	44	TLRKK…FKRGP → ALNKKEHRGCDSPDPDTSYV LTPHTEEKYKKINEEFDNMM RNHKIA in isoform 3.		VSP_026060
	Alternative sequence	287 – 294	8	Missing in isoform 2 and isoform 3.		VSP_026031
Experimental info
	Sequence conflict	98	1	S → N in AAA74030. Ref.1
	Sequence conflict	116	1	S → I in AAA74030. Ref.1
	Sequence conflict	133	1	L → F in AAA74030. Ref.1
	Sequence conflict	151	1	A → P in AAA74030. Ref.1
	Sequence conflict	154	1	Y → D in AAA74030. Ref.1
	Sequence conflict	174 – 175	2	DS → ET in AAA74030. Ref.1
	Sequence conflict	201	1	G → S in BAE21297. Ref.2
	Sequence conflict	274	1	V → A in AAA74030. Ref.1
	Sequence conflict	367	1	Q → E in AAA74030. Ref.1
	Sequence conflict	373 – 374	2	AA → TT in AAA74030. Ref.1
	Sequence conflict	419 – 423	5	QQQQQ → HHHHH in AAA74030. Ref.1
	Sequence conflict	478	1	P → A in AAA74030. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: FE291C3E3E0A5E70	FASTA	498	53,579
	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 TLADSSMLSP 190 200 210 220 230 240 PPATLHRNVS PGAPQRPPST GSASGMLSTT DLTVPNGAGN SPVGNGFVNS RASPNLIGNT 250 260 270 280 290 300 GANSLGKVMP TKSPPPPGGG SLGMNSRKPD LRVVIPPSSK GMMPPLSEEE ELELNAQRIS 310 320 330 340 350 360 SSQATQPLAT PVVSVTTPSL PPQGLVYSAM PTAYNTDYSL TSADLSALQG FTSPGMLSLG 370 380 390 400 410 420 QASAWQQHHL GQAALSSLVA GGQLSQGSNL SINTNQNINI KSEPISPPRD RMTPSGFQQQ 430 440 450 460 470 480 QQQPQQQPPP QPPQPQPRQE MGRSPVDSLS SSSSSYDGSD REDPRGDFHS PIVLGRPPNT 490 EDRESPSVKR MRMDTWVT
	Isoform 2 [UniParc]. Checksum: 2E15C204F58A9646	FASTA	490	52,620
	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 TLADSSMLSP 190 200 210 220 230 240 PPATLHRNVS PGAPQRPPST GSASGMLSTT DLTVPNGAGN SPVGNGFVNS RASPNLIGNT 250 260 270 280 290 300 GANSLGKVMP TKSPPPPGGG SLGMNSRKPD LRVVIPPSSK GMMPPLNAQR ISSSQATQPL 310 320 330 340 350 360 ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL QGFTSPGMLS LGQASAWQQH 370 380 390 400 410 420 HLGQAALSSL VAGGQLSQGS NLSINTNQNI NIKSEPISPP RDRMTPSGFQ QQQQQPQQQP 430 440 450 460 470 480 PPQPPQPQPR QEMGRSPVDS LSSSSSSYDG SDREDPRGDF HSPIVLGRPP NTEDRESPSV 490 KRMRMDTWVT
	Isoform 3 [UniParc]. Checksum: 961882F1C572ACCF	FASTA	492	52,990
	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 SSTLADSSML 190 200 210 220 230 240 SPPPATLHRN VSPGAPQRPP STGSASGMLS TTDLTVPNGA GNSPVGNGFV NSRASPNLIG 250 260 270 280 290 300 NTGANSLGKV MPTKSPPPPG GGSLGMNSRK PDLRVVIPPS SKGMMPPLNA QRISSSQATQ 310 320 330 340 350 360 PLATPVVSVT TPSLPPQGLV YSAMPTAYNT DYSLTSADLS ALQGFTSPGM LSLGQASAWQ 370 380 390 400 410 420 QHHLGQAALS SLVAGGQLSQ GSNLSINTNQ NINIKSEPIS PPRDRMTPSG FQQQQQQPQQ 430 440 450 460 470 480 QPPPQPPQPQ PRQEMGRSPV DSLSSSSSSY DGSDREDPRG DFHSPIVLGR PPNTEDRESP 490 SVKRMRMDTW VT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 (ISOFORM 1), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND THR-108 (ISOFORM 3), MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U30823 mRNA. Translation: AAA74030.1. AK132678 mRNA. Translation: BAE21297.1. BC061128 mRNA. Translation: AAH61128.1. BC096598 mRNA. Translation: AAH96598.1.
IPI	IPI00420437. IPI00465749. IPI00607917.
RefSeq	NP_001028885.1. NM_001033713.1.
UniGene	Mm.132788. Mm.426509.
3D structure databases
ProteinModelPortal	Q60929.
SMR	Q60929. Positions 2-73.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q60929. 1 interaction.
MINT	MINT-3155471.
STRING	10090.ENSMUSP00000117496.
PTM databases
PhosphoSite	Q60929.
Proteomic databases
PaxDb	Q60929.
PRIDE	Q60929.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032776; ENSMUSP00000032776; ENSMUSG00000030557. ENSMUST00000076325; ENSMUSP00000075664; ENSMUSG00000030557. ENSMUST00000107476; ENSMUSP00000103100; ENSMUSG00000030557. ENSMUST00000156690; ENSMUSP00000117496; ENSMUSG00000030557.
GeneID	17258.
KEGG	mmu:17258.
UCSC	uc009hie.1. mouse. uc009hif.1. mouse. uc009hig.1. mouse.
Organism-specific databases
CTD	4205.
MGI	MGI:99532. Mef2a.
Phylogenomic databases
eggNOG	COG5068.
GeneTree	ENSGT00390000011828.
HOGENOM	HOG000230620.
HOVERGEN	HBG053944.
InParanoid	Q60929.
KO	K09260.
OMA	RMDTWVT.
OrthoDB	EOG4XWFXW.
Gene expression databases
ArrayExpress	Q60929.
Bgee	Q60929.
CleanEx	MM_MEF2A.
Genevestigator	Q60929.
GermOnline	ENSMUSG00000030557. Mus musculus.
Family and domain databases
InterPro	IPR022102. HJURP_C. IPR002100. TF_MADSbox. [Graphical view]
Pfam	PF12347. HJURP_C. 1 hit. PF00319. SRF-TF. 1 hit. [Graphical view]
PRINTS	PR00404. MADSDOMAIN.
SMART	SM00432. MADS. 1 hit. [Graphical view]
SUPFAM	SSF55455. TF_MADSbox. 1 hit.
PROSITE	PS00350. MADS_BOX_1. 1 hit. PS50066. MADS_BOX_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MEF2A. mouse.
NextBio	291742.
SOURCE	Search...

Entry information

Entry name

MEF2A_MOUSE

Accession

Primary (citable) accession number: Q60929
Secondary accession number(s): Q3V155, Q4VA09, Q6P8Q3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 29, 2007
Last modified:	April 3, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program