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Protein

Myocyte-specific enhancer factor 2D

Gene

Mef2d

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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, 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. Plays a critical role in the regulation of neuronal apoptosis (By similarity).By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2D
Gene namesi
Name:Mef2d
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621489. Mef2d.

Subcellular locationi

  • Nucleus

  • Note: Translocated by HDAC4 to nuclear dots.By similarity

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Myocyte-specific enhancer factor 2DPRO_0000366974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981PhosphoserineCombined sources
Modified residuei106 – 1061PhosphoserineCombined sources
Modified residuei110 – 1101PhosphoserineBy similarity
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei180 – 1801PhosphoserineCombined sources
Modified residuei190 – 1901Phosphoserine; by PKABy similarity
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei245 – 2451N6-acetyllysineBy similarity
Modified residuei251 – 2511PhosphoserineCombined sources
Modified residuei425 – 4251N6-acetyllysine; alternateBy similarity
Cross-linki425 – 425Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Modified residuei430 – 4301PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on Ser-430 by CDK5 is required for Lys-425 sumoylation and inhibits transcriptional activity. In neurons, enhanced CDK5 activity induced by neurotoxins promotes caspase 3-mediated cleavage leading to neuron apoptosis. Phosphorylation on Ser-180 can be enhanced by EGF. Phosphorylated and activated by CaMK4 (By similarity).By similarity
Acetylated on Lys-425 by CREBBP. Acetylated by EP300. Deacetylated by SIRT1 and HDAC3 (By similarity).By similarity
Sumoylated on Lys-425 with SUMO2 but not SUMO1; which inhibits transcriptional activity and myogenic activity. Desumoylated by SENP3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO89038.
PRIDEiO89038.

PTM databases

iPTMnetiO89038.
PhosphoSiteiO89038.

Interactioni

Subunit structurei

Forms a complex with class II HDACs in undifferentiating cells. On myogenic differentiation, HDACs are released into the cytoplasm allowing MEF2s to interact with other proteins for activation. Interacts with HDAC4 (in undifferentiating cells); the interaction translocates MEF2D to nuclear dots (By similarity). Forms a heterodimer with MEF2A (By similarity). Interacts with MAPK7; the interaction phosphorylates but does not activate MEF2D (PubMed:9753748). Interacts with MYOG (By similarity). Interacts with CCAR2 and HDAC3 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi249515. 5 interactions.
STRINGi10116.ENSRNOP00000041061.

Structurei

3D structure databases

ProteinModelPortaliO89038.
SMRiO89038. Positions 2-92.
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 biasi252 – 2554Poly-Pro
Compositional biasi360 – 39031Gln/Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 MADS-box domain.PROSITE-ProRule annotation
Contains 1 Mef2-type DNA-binding domain.Curated

Phylogenomic databases

eggNOGiKOG0014. Eukaryota.
COG5068. LUCA.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiO89038.
KOiK09262.
OrthoDBiEOG793B7D.
PhylomeDBiO89038.

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]

Sequencei

Sequence statusi: Complete.

O89038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRKKIQIQR ITDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNH
60 70 80 90 100
SNKLFQYAST DMDKVLLKYT EYNEPHESRT NADIIETLRK KGFNGCDSPE
110 120 130 140 150
PDGEDSLEQS PLLEDKYRRA SEELDGLFRR YGSSVPAPNF AMPVTVPVSN
160 170 180 190 200
QSSMQFSNPS SSLVTPSLVT SSLTDPRLLS PQQPALQRNS VSPGLPQRPA
210 220 230 240 250
SAGAMLGRDL NSANGACPNP VGNGYVSARA SPGLLPVANG NGLNKVIPAK
260 270 280 290 300
SPPPPTHNTQ LGAPSRKPDL RVITSQGGKG LMHHLNNAQR LGVSQSTHSL
310 320 330 340 350
TTPVVSVATP SLLSQGLPFS SMPTAYNTDY QLPSAELSSL PAFSSPAGLA
360 370 380 390 400
LGNVTAWQQP QQPQQPQPPQ PPQSQPQPPQ PQPQQPPQQQ PHLVPVSLSN
410 420 430 440 450
LIPGSPLPHV GAALTVTTHP HISIKSEPVS PSRERSPAPP PPAVFPAARP
460 470 480 490 500
EPGEGLSSPA GGSYETGDRD DGRGDFGPTL GLLRPAPEPE AEGSAVKRMR

LDTWTLK
Length:507
Mass (Da):54,368
Last modified:November 1, 1998 - v1
Checksum:i303D4A865805FA41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081R → G in AAH81790 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005425 mRNA. Translation: CAA06531.1.
BC081790 mRNA. Translation: AAH81790.1.
RefSeqiNP_110487.2. NM_030860.2.
UniGeneiRn.89018.

Genome annotation databases

GeneIDi81518.
KEGGirno:81518.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005425 mRNA. Translation: CAA06531.1.
BC081790 mRNA. Translation: AAH81790.1.
RefSeqiNP_110487.2. NM_030860.2.
UniGeneiRn.89018.

3D structure databases

ProteinModelPortaliO89038.
SMRiO89038. Positions 2-92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249515. 5 interactions.
STRINGi10116.ENSRNOP00000041061.

PTM databases

iPTMnetiO89038.
PhosphoSiteiO89038.

Proteomic databases

PaxDbiO89038.
PRIDEiO89038.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81518.
KEGGirno:81518.

Organism-specific databases

CTDi4209.
RGDi621489. Mef2d.

Phylogenomic databases

eggNOGiKOG0014. Eukaryota.
COG5068. LUCA.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiO89038.
KOiK09262.
OrthoDBiEOG793B7D.
PhylomeDBiO89038.

Miscellaneous databases

PROiO89038.

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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAPK7.
    Strain: Wistar.
    Tissue: Heart.
  2. "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].
    Tissue: Testis.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-106; SER-121; SER-180; SER-231 AND SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMEF2D_RAT
AccessioniPrimary (citable) accession number: O89038
Secondary accession number(s): Q66HL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 100 of the entry and version 1 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. 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.