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Protein

Myocyte-specific enhancer factor 2

Gene

Mef2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that could be a key player in early mesoderm differentiation and may be required for subsequent cell fate specifications within the somatic and visceral/heart mesodermal layers.3 Publications

Regions

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

GO - Molecular functioni

  • DNA binding Source: FlyBase
  • enhancer sequence-specific DNA binding Source: FlyBase
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: FlyBase
  • transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: FlyBase

GO - Biological processi

  • anterior midgut development Source: FlyBase
  • antimicrobial humoral response Source: FlyBase
  • carbohydrate storage Source: FlyBase
  • heart development Source: FlyBase
  • lipid storage Source: FlyBase
  • locomotor rhythm Source: FlyBase
  • mesoderm development Source: FlyBase
  • muscle fiber development Source: FlyBase
  • muscle organ development Source: FlyBase
  • myoblast fusion Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: FlyBase
  • regulation of gene expression Source: FlyBase
  • regulation of striated muscle tissue development Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • skeletal muscle tissue development Source: FlyBase
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-375170. CDO in myogenesis.
SignaLinkiP40791.

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2
Short name:
D-mef2
Alternative name(s):
MADS domain transcription factor
Gene namesi
Name:Mef2
ORF Names:CG1429
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0011656. Mef2.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540Myocyte-specific enhancer factor 2PRO_0000199427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 951Phosphoserine1 Publication
Modified residuei98 – 981Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiP40791.

Expressioni

Tissue specificityi

Expressed in all presumptive mesoderm prior to the splitting process that generates the somatic and visceral/ heart mesoderm. After the subdivision, it is found in both the somatic and the visceral/heart mesoderm.3 Publications

Developmental stagei

First detectable in the presumptive mesoderm at late cellular blastoderm stage.2 Publications

Inductioni

TWI activity is required for MEF2 expression. SNA activity is needed for maintaining MEF2 expression.

Gene expression databases

BgeeiP40791.
ExpressionAtlasiP40791. differential.
GenevisibleiP40791. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TbpP202272EBI-235994,EBI-169179

Protein-protein interaction databases

BioGridi61860. 5 interactions.
IntActiP40791. 1 interaction.
MINTiMINT-994108.

Structurei

3D structure databases

ProteinModelPortaliP40791.
SMRiP40791. Positions 2-73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi377 – 43155Gly-richAdd
BLAST
Compositional biasi380 – 3867Poly-Ser
Compositional biasi390 – 3967Poly-Gly
Compositional biasi419 – 42810Poly-Gly
Compositional biasi508 – 5136Poly-Gln
Compositional biasi516 – 5194Poly-Gln

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

GeneTreeiENSGT00390000011828.
HOGENOMiHOG000263901.
InParanoidiP40791.
KOiK09263.
OrthoDBiEOG7CRTQ1.
PhylomeDBiP40791.

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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform D (identifier: P40791-1) [UniParc]FASTAAdd to basket

Also known as: 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.

« Hide

        10         20         30         40         50
MGRKKIQISR ITDERNRQVT FNKRKFGVMK KAYELSVLCD CEIALIIFSS
60 70 80 90 100
SNKLYQYAST DMDRVLLKYT EYNEPHESLT NKNIIEKENK NGVMSPDSPE
110 120 130 140 150
AETDYTLTPR TEAKYNKIDE EFQNMMQRNQ MAIGGAGAPR QLPNSSYTLP
160 170 180 190 200
VSVPVPGSYG DNLLQASPQM SHTNISPRPS SSETDSGGMS LIIYPSGSML
210 220 230 240 250
EMSNGYPHSH SPLVGSPSPG PSPGIAHHLS IKQQSPGSQN GRASNLRVVI
260 270 280 290 300
PPTIAPIPPN MSAPDDVGYA DQRQSQTSLN TPVVTLQTPI PALTSYSFGA
310 320 330 340 350
QDFSSSGVMN SADIMSLNTW HQGLVPHSSL SHLAVSNSTP PPATSPVSIK
360 370 380 390 400
VKAEPQSPPR DLSASGHQQN SNGSTGSGGS SSSTSSNASG GAGGGGAVSA
410 420 430 440 450
ANVITHLNNV SVLAGGPSGQ GGGGGGGGSN GNVEQATNLS VLSHAQQHHL
460 470 480 490 500
GMPNSRPSST GHITPTPGHD KYEGYPYRAL MGHNPRWNLN FAGAPSSDQD
510 520 530 540
VRLAAVAVQQ QQQQPHQQQQ LGDYDAPNHK RPRISGGWGT
Length:540
Mass (Da):57,172
Last modified:October 19, 2011 - v3
Checksum:i0B82D0C61EE1899E
GO
Isoform A (identifier: P40791-2) [UniParc]FASTAAdd to basket

Also known as: 3

The sequence of this isoform differs from the canonical sequence as follows:
     187-193: GGMSLII → V
     468-491: GHDKYEGYPYRALMGHNPRWNLNF → DFIILN

Show »
Length:516
Mass (Da):54,397
Checksum:i9514C616F8FCAA49
GO
Isoform B (identifier: P40791-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     187-193: GGMSLII → V
     469-493: Missing.

Note: No experimental confirmation available.
Show »
Length:509
Mass (Da):53,610
Checksum:iFDAC8DD1D4458F11
GO
Isoform C (identifier: P40791-4) [UniParc]FASTAAdd to basket

Also known as: 2

The sequence of this isoform differs from the canonical sequence as follows:
     469-493: Missing.

Show »
Length:515
Mass (Da):54,183
Checksum:iFC282A1CAAE3F614
GO
Isoform F (identifier: P40791-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     187-225: Missing.

Note: No experimental confirmation available.
Show »
Length:501
Mass (Da):53,294
Checksum:i15E435B57713126C
GO

Sequence cautioni

The sequence AAL28644.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAM48340.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 33MGR → WAA in AAL28644 (PubMed:12537569).Curated
Sequence conflicti1 – 33MGR → WAA in AAM48340 (PubMed:12537569).Curated
Sequence conflicti97 – 971D → E in AAF06817 (PubMed:7839146).Curated
Sequence conflicti101 – 1011A → G in AAF06817 (PubMed:7839146).Curated
Sequence conflicti112 – 1143EAK → GGM in AAF06817 (PubMed:7839146).Curated
Sequence conflicti338 – 3381S → R in AAA20463 (PubMed:8052612).Curated
Sequence conflicti364 – 37714ASGHQ…GSTGS → PAVISRIAMVPRAG in AAA19957 (PubMed:8202544).CuratedAdd
BLAST
Sequence conflicti364 – 37714ASGHQ…GSTGS → PAVISRIAMVPRAG in AAF06817 (PubMed:7839146).CuratedAdd
BLAST
Sequence conflicti429 – 4291S → T in AAF06817 (PubMed:7839146).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei187 – 22539Missing in isoform F. 1 PublicationVSP_041851Add
BLAST
Alternative sequencei187 – 1937GGMSLII → V in isoform A and isoform B. 1 PublicationVSP_006237
Alternative sequencei468 – 49124GHDKY…WNLNF → DFIILN in isoform A. 1 PublicationVSP_006238Add
BLAST
Alternative sequencei469 – 49325Missing in isoform B and isoform C. 4 PublicationsVSP_006239Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03292 mRNA. Translation: AAA19957.1.
U07422 mRNA. Translation: AAA20463.1.
X83527 mRNA. Translation: CAA58508.1.
U19493 Genomic DNA. Translation: AAF06817.1.
AE013599 Genomic DNA. Translation: AAF58872.1.
AE013599 Genomic DNA. Translation: AAM71042.1.
AE013599 Genomic DNA. Translation: AAM71043.1.
AE013599 Genomic DNA. Translation: AAM71044.1.
AE013599 Genomic DNA. Translation: AAS64881.1.
AY061096 mRNA. Translation: AAL28644.1. Different initiation.
AY061589 mRNA. Translation: AAL29137.1.
AY118311 mRNA. Translation: AAM48340.1. Different initiation.
RefSeqiNP_477018.1. NM_057670.5. [P40791-4]
NP_477019.1. NM_057671.5. [P40791-3]
NP_477020.1. NM_057672.5. [P40791-1]
NP_477021.1. NM_057673.5. [P40791-2]
NP_995789.1. NM_206067.4. [P40791-6]
UniGeneiDm.7054.

Genome annotation databases

EnsemblMetazoaiFBtr0088443; FBpp0087529; FBgn0011656. [P40791-1]
GeneIDi36032.
KEGGidme:Dmel_CG1429.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03292 mRNA. Translation: AAA19957.1.
U07422 mRNA. Translation: AAA20463.1.
X83527 mRNA. Translation: CAA58508.1.
U19493 Genomic DNA. Translation: AAF06817.1.
AE013599 Genomic DNA. Translation: AAF58872.1.
AE013599 Genomic DNA. Translation: AAM71042.1.
AE013599 Genomic DNA. Translation: AAM71043.1.
AE013599 Genomic DNA. Translation: AAM71044.1.
AE013599 Genomic DNA. Translation: AAS64881.1.
AY061096 mRNA. Translation: AAL28644.1. Different initiation.
AY061589 mRNA. Translation: AAL29137.1.
AY118311 mRNA. Translation: AAM48340.1. Different initiation.
RefSeqiNP_477018.1. NM_057670.5. [P40791-4]
NP_477019.1. NM_057671.5. [P40791-3]
NP_477020.1. NM_057672.5. [P40791-1]
NP_477021.1. NM_057673.5. [P40791-2]
NP_995789.1. NM_206067.4. [P40791-6]
UniGeneiDm.7054.

3D structure databases

ProteinModelPortaliP40791.
SMRiP40791. Positions 2-73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61860. 5 interactions.
IntActiP40791. 1 interaction.
MINTiMINT-994108.

PTM databases

iPTMnetiP40791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088443; FBpp0087529; FBgn0011656. [P40791-1]
GeneIDi36032.
KEGGidme:Dmel_CG1429.

Organism-specific databases

CTDi36032.
FlyBaseiFBgn0011656. Mef2.

Phylogenomic databases

GeneTreeiENSGT00390000011828.
HOGENOMiHOG000263901.
InParanoidiP40791.
KOiK09263.
OrthoDBiEOG7CRTQ1.
PhylomeDBiP40791.

Enzyme and pathway databases

ReactomeiR-DME-375170. CDO in myogenesis.
SignaLinkiP40791.

Miscellaneous databases

GenomeRNAii36032.
PROiP40791.

Gene expression databases

BgeeiP40791.
ExpressionAtlasiP40791. differential.
GenevisibleiP40791. DM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "D-MEF2: a MADS box transcription factor expressed in differentiating mesoderm and muscle cell lineages during Drosophila embryogenesis."
    Lilly B., Galewsky S., Firulli A.B., Schulz R.A., Olson E.N.
    Proc. Natl. Acad. Sci. U.S.A. 91:5662-5666(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. "D-mef2: a Drosophila mesoderm-specific MADS box-containing gene with a biphasic expression profile during embryogenesis."
    Nguyen H.T., Bodmer R., Abmayr S.M., McDermott J.C., Spoerel N.A.
    Proc. Natl. Acad. Sci. U.S.A. 91:7520-7524(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  3. "Drosophila MEF2 is regulated by twist and is expressed in both the primordia and differentiated cells of the embryonic somatic, visceral and heart musculature."
    Taylor M.V., Beatty K.E., Hunter H.K., Baylies M.K.
    Mech. Dev. 50:29-41(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C AND D), TISSUE SPECIFICITY.
    Tissue: Embryo.
  4. "Requirement of MADS domain transcription factor D-MEF2 for muscle formation in Drosophila."
    Lilly B., Zhao B., Ranganayakulu G., Paterson B.M., Schulz R.A., Olson E.N.
    Science 267:688-693(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  5. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  6. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  7. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND F), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-192 (ISOFORMS C/D).
    Strain: Berkeley.
    Tissue: Embryo and Head.
  8. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-98, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiMEF2_DROME
AccessioniPrimary (citable) accession number: P40791
Secondary accession number(s): A1Z821
, Q24394, Q8MT88, Q95R70, Q95RW1, Q9U5I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 19, 2011
Last modified: June 8, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.