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Protein

Myocyte-specific enhancer factor 2C

Gene

MEF2C

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi58 – 86Mef2-typeSequence analysisAdd BLAST29

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2C
Gene namesi
Name:MEF2C
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003669731 – 463Myocyte-specific enhancer factor 2CAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4N6-acetyllysineBy similarity1
Modified residuei59Phosphoserine; by CK2By similarity1
Modified residuei98PhosphoserineBy similarity1
Modified residuei104PhosphoserineBy similarity1
Modified residuei114N6-acetyllysineBy similarity1
Modified residuei117N6-acetyllysineBy similarity1
Modified residuei220PhosphoserineBy similarity1
Modified residuei226PhosphoserineBy similarity1
Modified residuei232N6-acetyllysineBy similarity1
Modified residuei237N6-acetyllysineBy similarity1
Modified residuei238PhosphoserineBy similarity1
Modified residuei250N6-acetyllysineBy similarity1
Modified residuei262N6-acetyllysineBy similarity1
Modified residuei283Phosphothreonine; by MAPK7 and MAPK14By similarity1
Modified residuei290Phosphothreonine; by MAPK7 and MAPK14By similarity1
Cross-linki381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei386Phosphoserine; by CDK5By similarity1
Modified residuei409Phosphoserine; by MAPK7By similarity1
Modified residuei435PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated on Ser-59; which enhances DNA binding activity. Phosphorylated on Ser-386; which is required for Lys-381 sumoylation and inhibits transcriptional activity.By similarity
Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity).By similarity
Sumoylated on Lys-381 with SUMO2 but not SUMO1; which represses transcriptional activity.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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei422 – 423CleavageCurated2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiA4UTP7.

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 EP300 in differentiating cells; the interaction acetylates MEF2C leading to increased DNA binding and activation (By similarity). Interacts with HDAC7 and CARM1 (By similarity). Interacts with HDAC4 and HDAC9; the interaction with HDACs represses transcriptional activity (By similarity). Interacts with LPIN1. Interacts with MYOCD. Interacts with AKAP13 (By similarity). Interacts with FOXK1; the interaction inhibits MEF2C transactivation activity (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015044.

Structurei

3D structure databases

ProteinModelPortaliA4UTP7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 57MADS-boxPROSITE-ProRule annotationAdd BLAST55

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni358 – 389Transcription repressorBy similarityAdd BLAST32

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.
InParanoidiA4UTP7.
KOiK04454.

Family and domain databases

CDDicd00265. MADS_MEF2_like. 1 hit.
InterProiIPR022102. HJURP_C.
IPR033896. MADS_MEF2-like.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A4UTP7-1) [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
TNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVEALNK KENKGCESPD
110 120 130 140 150
PDSSYALTPR TEEKYKKINE EFDNMIKSHK IPAVPPPNFE MPVSIPVSSH
160 170 180 190 200
NSLVYSNPVS SLGNPNFLPL AHPSLQRNSM SPGVTHRPPS AGNTGGLMGG
210 220 230 240 250
DLTSGAGTSA GNGYGNPRNS PGLLVSPGNL NKNMQAKSPP PMNLGMNNRK
260 270 280 290 300
PDLRVLIPPG SKNTMPSVSQ RINNSQSAQS LATPVVSVAT PTLPGQGMGG
310 320 330 340 350
YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP
360 370 380 390 400
SALSQLGACT STHLSQSSNL SLPSTQSLNI KSEPVSPPRD RTTTPSRYPQ
410 420 430 440 450
HTRHEAGRSP VDSLSSCSSS YDGSDREDHR NEFHSPIGLT RPSPDERESP
460
SVKRMRLSEG WAT
Length:463
Mass (Da):50,249
Last modified:May 15, 2007 - v1
Checksum:i76BA0222D9996114
GO
Isoform 2 (identifier: A4UTP7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: ALNKKENKGC...DNMIKSHKIP → TLRKKGLNGC...DLMISRQRLC
     358-389: Missing.

Show »
Length:433
Mass (Da):46,994
Checksum:i62CC5623EA0F0D21
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti167F → L in ABC68473 (Ref. 1) Curated1
Sequence conflicti269S → N in ABC68473 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03660087 – 132ALNKK…SHKIP → TLRKKGLNGCDSPDPDADDS VGHSPESEDKYRKINEDLDL MISRQRLC in isoform 2. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_036601358 – 389Missing in isoform 2. 1 PublicationAdd BLAST32

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ343149 mRNA. Translation: ABC68473.1.
EF486522 mRNA. Translation: ABO77944.1.
RefSeqiNP_001038005.1. NM_001044540.1.
UniGeneiSsc.34788.

Genome annotation databases

GeneIDi733590.
KEGGissc:733590.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ343149 mRNA. Translation: ABC68473.1.
EF486522 mRNA. Translation: ABO77944.1.
RefSeqiNP_001038005.1. NM_001044540.1.
UniGeneiSsc.34788.

3D structure databases

ProteinModelPortaliA4UTP7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015044.

Proteomic databases

PaxDbiA4UTP7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi733590.
KEGGissc:733590.

Organism-specific databases

CTDi4208.

Phylogenomic databases

eggNOGiKOG0014. Eukaryota.
COG5068. LUCA.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiA4UTP7.
KOiK04454.

Family and domain databases

CDDicd00265. MADS_MEF2_like. 1 hit.
InterProiIPR022102. HJURP_C.
IPR033896. MADS_MEF2-like.
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...

Entry informationi

Entry nameiMEF2C_PIG
AccessioniPrimary (citable) accession number: A4UTP7
Secondary accession number(s): Q2L9Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 15, 2007
Last modified: November 30, 2016
This is version 60 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.