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UniProtKB - Q8CFN5 (MEF2C_MOUSE)

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Protein

Myocyte-specific enhancer factor 2C

Gene

Mef2c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. May also be involved in neurogenesis and in the development of cortical architecture. Isoform 3 and isoform 4, which lack the repressor domain, are more active than isoform 1, isoform 2 and isoform 5 (By similarity). 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.By similarity7 Publications

Regions

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

GO - Molecular functioni

  • activating transcription factor binding Source: MGI
  • AT DNA binding Source: MGI
  • chromatin binding Source: MGI
  • core promoter proximal region sequence-specific DNA binding Source: MGI
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • DNA binding Source: MGI
  • histone deacetylase binding Source: BHF-UCL
  • HMG box domain binding Source: UniProtKB
  • miRNA binding Source: UniProtKB
  • protein heterodimerization activity Source: MGI
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding Source: NTNU_SB
  • transcription factor activity, RNA polymerase II core promoter sequence-specific Source: UniProtKB
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: MGI
  • transcription factor activity, sequence-specific DNA binding Source: MGI
  • transcription regulatory region DNA binding Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • B cell homeostasis Source: UniProtKB
  • B cell proliferation Source: UniProtKB
  • B cell receptor signaling pathway Source: UniProtKB
  • blood vessel development Source: MGI
  • blood vessel remodeling Source: MGI
  • cardiac muscle cell differentiation Source: MGI
  • cardiac muscle hypertrophy in response to stress Source: MGI
  • cardiac ventricle formation Source: UniProtKB
  • cartilage morphogenesis Source: MGI
  • cell fate commitment Source: MGI
  • cell morphogenesis involved in neuron differentiation Source: Alzheimers_University_of_Toronto
  • cellular response to calcium ion Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • cellular response to fluid shear stress Source: UniProtKB
  • cellular response to glucose stimulus Source: Ensembl
  • cellular response to lipopolysaccharide Source: UniProtKB
  • cellular response to parathyroid hormone stimulus Source: UniProtKB
  • cellular response to retinoic acid Source: Ensembl
  • cellular response to transforming growth factor beta stimulus Source: UniProtKB
  • cellular response to trichostatin A Source: UniProtKB
  • chondrocyte differentiation Source: MGI
  • dentate gyrus development Source: Ensembl
  • embryonic skeletal system morphogenesis Source: MGI
  • embryonic viscerocranium morphogenesis Source: MGI
  • endochondral ossification Source: MGI
  • epithelial cell proliferation involved in renal tubule morphogenesis Source: UniProtKB
  • excitatory postsynaptic potential Source: Alzheimers_University_of_Toronto
  • germinal center formation Source: UniProtKB
  • glomerulus morphogenesis Source: UniProtKB
  • heart development Source: MGI
  • heart looping Source: UniProtKB
  • humoral immune response Source: UniProtKB
  • learning or memory Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • melanocyte differentiation Source: UniProtKB
  • monocyte differentiation Source: MGI
  • muscle cell fate determination Source: MGI
  • myotube differentiation Source: Ensembl
  • negative regulation of epithelial cell proliferation Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • negative regulation of ossification Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • nephron tubule epithelial cell differentiation Source: UniProtKB
  • neural crest cell differentiation Source: UniProtKB
  • neuron development Source: UniProtKB
  • neuron differentiation Source: UniProtKB
  • neuron migration Source: Alzheimers_University_of_Toronto
  • osteoblast differentiation Source: MGI
  • outflow tract morphogenesis Source: MGI
  • palate development Source: MGI
  • platelet formation Source: UniProtKB
  • positive regulation of alkaline phosphatase activity Source: UniProtKB
  • positive regulation of B cell proliferation Source: UniProtKB
  • positive regulation of behavioral fear response Source: UniProtKB
  • positive regulation of bone mineralization Source: UniProtKB
  • positive regulation of cardiac muscle cell differentiation Source: UniProtKB
  • positive regulation of cardiac muscle cell proliferation Source: UniProtKB
  • positive regulation of cell proliferation in bone marrow Source: MGI
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of macrophage apoptotic process Source: UniProtKB
  • positive regulation of MAP kinase activity Source: Alzheimers_University_of_Toronto
  • positive regulation of myoblast differentiation Source: UniProtKB
  • positive regulation of neuron differentiation Source: UniProtKB
  • positive regulation of osteoblast differentiation Source: UniProtKB
  • positive regulation of protein homodimerization activity Source: MGI
  • positive regulation of skeletal muscle cell differentiation Source: MGI
  • positive regulation of skeletal muscle tissue development Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • primary heart field specification Source: UniProtKB
  • regulation of AMPA receptor activity Source: Alzheimers_University_of_Toronto
  • regulation of dendritic spine development Source: Alzheimers_University_of_Toronto
  • regulation of germinal center formation Source: UniProtKB
  • regulation of megakaryocyte differentiation Source: UniProtKB
  • regulation of neuron apoptotic process Source: Alzheimers_University_of_Toronto
  • regulation of neurotransmitter secretion Source: Alzheimers_University_of_Toronto
  • regulation of NMDA receptor activity Source: Alzheimers_University_of_Toronto
  • regulation of sarcomere organization Source: MGI
  • regulation of synapse assembly Source: Alzheimers_University_of_Toronto
  • regulation of synaptic activity Source: UniProtKB
  • regulation of synaptic plasticity Source: Alzheimers_University_of_Toronto
  • regulation of synaptic transmission, glutamatergic Source: Alzheimers_University_of_Toronto
  • regulation of transcription, DNA-templated Source: MGI
  • renal tubule morphogenesis Source: UniProtKB
  • response to ischemia Source: Alzheimers_University_of_Toronto
  • response to virus Source: Ensembl
  • response to vitamin E Source: Ensembl
  • secondary heart field specification Source: UniProtKB
  • sinoatrial valve morphogenesis Source: UniProtKB
  • skeletal muscle cell differentiation Source: MGI
  • skeletal muscle tissue development Source: MGI
  • smooth muscle cell differentiation Source: MGI
  • transdifferentiation Source: Ensembl
  • ventricular cardiac muscle cell differentiation Source: UniProtKB
Complete GO annotation...

Keywordsi

Molecular functionActivator, Developmental protein, DNA-binding
Biological processApoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-375170. CDO in myogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2C
Gene namesi
Name:Mef2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:99458. Mef2c.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice show impairment in hippocampal-dependent learning and also increase in the number of excitatory synapses and potentiation of basal and evoked synaptic transmission. Mice surviving to adulthood manifest smaller, apparently less mature neurons and smaller whole brain size, with resultant aberrant electrophysiology and behavior. Mice exhibit thrombocytopenia and a defect in B-lymphopoiesis.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3R → T: Increased mobility in differentiating cells. Greatly reduced DNA binding. 1 Publication1
Mutagenesisi4K → Q: 7-fold increase in DNA binding. 1 Publication1
Mutagenesisi4K → R: Reduced acetylation by 30%. Some loss of DNA binding and transactivation activity. 1 Publication1
Mutagenesisi59 – 60ST → CR: Reduced DNA binding activity. 2
Mutagenesisi59 – 60ST → DD: Enhanced DNA binding activity. 2
Mutagenesisi59S → A: Reduced DNA binding activity. 1 Publication1
Mutagenesisi59S → D: Enhanced DNA binding activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001994341 – 474Myocyte-specific enhancer factor 2CAdd BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4N6-acetyllysine1 Publication1
Modified residuei59Phosphoserine; by CK21 Publication1
Modified residuei98PhosphoserineCombined sources1
Modified residuei106PhosphoserineCombined sources1
Modified residuei110PhosphoserineCombined sources1
Modified residuei116N6-acetyllysineBy similarity1
Modified residuei119N6-acetyllysineBy similarity1
Modified residuei222PhosphoserineCombined sources1
Modified residuei228PhosphoserineBy similarity1
Modified residuei234N6-acetyllysineBy similarity1
Modified residuei239N6-acetyllysineBy similarity1
Modified residuei240PhosphoserineCombined sources1
Modified residuei252N6-acetyllysineBy similarity1
Modified residuei264N6-acetyllysineBy similarity1
Modified residuei293Phosphothreonine; by MAPK14By similarity1
Modified residuei300Phosphothreonine; by MAPK14By similarity1
Cross-linki391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei396Phosphoserine; by CDK5By similarity1
Modified residuei420Phosphoserine; by MAPK7By similarity1
Modified residuei446PhosphoserineBy similarity1
Isoform 4 (identifier: Q8CFN5-4)
Modified residuei108PhosphothreonineCombined sources1
Isoform 5 (identifier: Q8CFN5-5)
Modified residuei108PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylation on Ser-59 enhances DNA binding activity (By similarity). Phosphorylation on Ser-396 is required for Lys-391 sumoylation and inhibits transcriptional activity.By similarity1 Publication
Acetylated by p300 on several sites in diffentiating myocytes (By similarity). Acetylation on Lys-4 increases DNA binding and transactivation.By similarity1 Publication
Sumoylated on Lys-391 with SUMO2 but not by SUMO1 represses transcriptional activity.By similarity
Proteolytically cleaved in cerebellar granule neurons, probably by 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
Sitei433 – 434CleavageCurated2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ8CFN5.
PeptideAtlasiQ8CFN5.
PRIDEiQ8CFN5.

PTM databases

iPTMnetiQ8CFN5.
PhosphoSitePlusiQ8CFN5.

Expressioni

Tissue specificityi

Widely expressed though mainly restricted to skeletal and cardiac muscle, brain, neurons and lymphocytes. Beta beta domain-lacking isoforms are the most predominantly expressed in all tissues including skeletal and cardiac muscle and brain. Only brain expresses all isoforms. Expression occurs primarily in the internal granule cell layer of the olfactory bulb, cortex, thalamus, hippocampus and cerebellum. Low levels in the cerebellum and hindbrain. Expressed throughout the cortex, including the frontal and entorhinal cortex, dentate gyrus, and basolateral amygdala. Selectively expressed in B-cells but not in T-cells, and its expression increases as B-cells mature.6 Publications

Developmental stagei

Expressed in developing endothelial cells and smooth muscle cells, as well as in surrounding mesenchyme, during embryogenesis. Up-regulated during myogenesis.1 Publication

Gene expression databases

BgeeiENSMUSG00000005583.
CleanExiMM_MEF2C.
ExpressionAtlasiQ8CFN5. baseline and differential.
GenevisibleiQ8CFN5. MM.

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 (PubMed:11279209, PubMed:11713257). Interacts with HDAC4, HDAC7 AND HDAC9; the interaction with HDACs represses transcriptional activity (By similarity). Interacts with LPIN1 (PubMed:19753306). Interacts with MYOCD (PubMed:16818234). Interacts with AKAP13 (PubMed:20139090). Interacts with FOXK1; the interaction inhibits MEF2C transactivation activity (PubMed:22956541).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AclyQ91V923EBI-643822,EBI-644049

GO - Molecular functioni

  • activating transcription factor binding Source: MGI
  • histone deacetylase binding Source: BHF-UCL
  • HMG box domain binding Source: UniProtKB
  • protein heterodimerization activity Source: MGI
Complete GO annotation...

Protein-protein interaction databases

BioGridi201383. 12 interactors.
DIPiDIP-49524N.
IntActiQ8CFN5. 6 interactors.
MINTiMINT-1551742.
STRINGi10090.ENSMUSP00000132547.

Structurei

Secondary structure

1474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 38Combined sources17
Beta strandi42 – 48Combined sources7
Beta strandi54 – 60Combined sources7
Helixi62 – 70Combined sources9
Beta strandi77 – 79Combined sources3
Helixi81 – 88Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5F28X-ray2.90A/B/C/D1-95[»]
ProteinModelPortaliQ8CFN5.
SMRiQ8CFN5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni271 – 278Beta domainBy similarity8
Regioni368 – 399Transcription repressorBy similarityAdd BLAST32

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 31Lys-rich (basic)Add BLAST28
Compositional biasi146 – 183Ser-richAdd BLAST38

Domaini

The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity.By similarity

Sequence similaritiesi

Belongs to the MEF2 family.Curated

Phylogenomic databases

eggNOGiKOG0014. Eukaryota.
COG5068. LUCA.
GeneTreeiENSGT00390000011828.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiQ8CFN5.
KOiK04454.
PhylomeDBiQ8CFN5.
TreeFamiTF314067.

Family and domain databases

CDDicd00265. MADS_MEF2_like. 1 hit.
Gene3Di3.40.1810.10. 1 hit.
InterProiView protein in InterPro
IPR022102. HJURP_C.
IPR033896. MADS_MEF2-like.
IPR002100. TF_MADSbox.
PfamiView protein in Pfam
PF12347. HJURP_C. 1 hit.
PF00319. SRF-TF. 1 hit.
PRINTSiPR00404. MADSDOMAIN.
SMARTiView protein in SMART
SM00432. MADS. 1 hit.
SUPFAMiSSF55455. SSF55455. 1 hit.
PROSITEiView protein in PROSITE
PS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

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

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q8CFN5-1) [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 NSDIVETLRK KGLNGCDSPD 
       110        120        130        140        150
PDADDSVGHS PESEDKYRKI NEDIDLMISR QRLCAVPPPS FEMPVTIPVS 
       160        170        180        190        200
SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN SMSPGVTHRP PSAGNTGGLM 
       210        220        230        240        250
GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS PPPMNLGMNN 
       260        270        280        290        300
RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT 
       310        320        330        340        350
PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW 
       360        370        380        390        400
QQQHLHNMPP SALSQLGACT STHLSQSSNL SLPSTQSLSI KSEPVSPPRD 
       410        420        430        440        450
RTTTPSRYPQ HTTRHEAGRS PVDSLSSCSS SYDGSDREDH RNEFHSPIGL 
       460        470 
TRPSPDERES PSVKRMRLSE GWAT
Note: No experimental confirmation available.
Length:474
Mass (Da):51,278
Last modified:January 4, 2005 - v2
Checksum:iCEFC2DB21E89632A
GO
Isoform 2 (identifier: Q8CFN5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     271-278: Missing.

Show »
Length:466
Mass (Da):50,393
Checksum:iF06A89C9ACD779AE
GO
Isoform 3 (identifier: Q8CFN5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     368-399: Missing.

Show »
Length:442
Mass (Da):47,956
Checksum:i40EFBF02BF3E775C
GO
Isoform 4 (identifier: Q8CFN5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-97: TLRKKGLNGCD → ALNKKENKGSE
     103-118: ADDSVGHSPESEDKYR → SSYALTPRTEEKYK
     123-134: DIDLMISRQRLC → EFDNMIKSHKIP
     271-278: Missing.
     368-399: Missing.

Show »
Length:432
Mass (Da):46,961
Checksum:iDCB2EBCE61A35215
GO
Isoform 5 (identifier: Q8CFN5-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-97: TLRKKGLNGCD → ALNKKENKGSE
     103-118: ADDSVGHSPESEDKYR → SSYALTPRTEEKYK
     123-134: DIDLMISRQRLC → EFDNMIKSHKIP

Show »
Length:472
Mass (Da):51,168
Checksum:i1B618AB137809260
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti141F → L in AAH37731 (PubMed:15489334).Curated1
Sequence conflicti211S → P (PubMed:8506376).Curated1
Sequence conflicti428C → S (PubMed:8506376).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01250187 – 97TLRKKGLNGCD → ALNKKENKGSE in isoform 4 and isoform 5. 2 PublicationsAdd BLAST11
Alternative sequenceiVSP_012502103 – 118ADDSV…EDKYR → SSYALTPRTEEKYK in isoform 4 and isoform 5. 2 PublicationsAdd BLAST16
Alternative sequenceiVSP_012503123 – 134DIDLM…RQRLC → EFDNMIKSHKIP in isoform 4 and isoform 5. 2 PublicationsAdd BLAST12
Alternative sequenceiVSP_012504271 – 278Missing in isoform 2 and isoform 4. 2 Publications8
Alternative sequenceiVSP_012505368 – 399Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST32

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009139 mRNA. Translation: BAB26099.1.
BC026841 mRNA. Translation: AAH26841.1.
BC037731 mRNA. Translation: AAH37731.1.
BC057650 mRNA. Translation: AAH57650.1.
CCDSiCCDS26664.1. [Q8CFN5-4]
CCDS49320.1. [Q8CFN5-2]
CCDS84042.1. [Q8CFN5-1]
CCDS84043.1. [Q8CFN5-3]
CCDS84045.1. [Q8CFN5-5]
RefSeqiNP_001334493.1. NM_001347564.1. [Q8CFN5-1]
NP_001334495.1. NM_001347566.1. [Q8CFN5-1]
NP_001334496.1. NM_001347567.1. [Q8CFN5-1]
NP_001334497.1. NM_001347568.1. [Q8CFN5-5]
NP_001334498.1. NM_001347569.1. [Q8CFN5-5]
NP_001334500.1. NM_001347571.1. [Q8CFN5-3]
NP_001334501.1. NM_001347572.1. [Q8CFN5-3]
NP_001334502.1. NM_001347573.1. [Q8CFN5-3]
NP_001334503.1. NM_001347574.1. [Q8CFN5-3]
NP_001334504.1. NM_001347575.1. [Q8CFN5-3]
NP_001334505.1. NM_001347576.1. [Q8CFN5-3]
NP_001334506.1. NM_001347577.1. [Q8CFN5-3]
NP_079558.1. NM_025282.3. [Q8CFN5-4]
XP_006517186.1. XM_006517123.2. [Q8CFN5-1]
XP_006517187.1. XM_006517124.3. [Q8CFN5-1]
XP_006517189.1. XM_006517126.2. [Q8CFN5-5]
XP_006517195.1. XM_006517132.3. [Q8CFN5-4]
XP_011242794.1. XM_011244492.2. [Q8CFN5-1]
XP_017170894.1. XM_017315405.1. [Q8CFN5-1]
UniGeneiMm.24001.
Mm.451574.
Mm.487610.

Genome annotation databases

EnsembliENSMUST00000185052; ENSMUSP00000138826; ENSMUSG00000005583. [Q8CFN5-5]
ENSMUST00000197146; ENSMUSP00000143227; ENSMUSG00000005583. [Q8CFN5-3]
ENSMUST00000197681; ENSMUSP00000143420; ENSMUSG00000005583. [Q8CFN5-3]
ENSMUST00000198199; ENSMUSP00000143742; ENSMUSG00000005583. [Q8CFN5-4]
ENSMUST00000199019; ENSMUSP00000143401; ENSMUSG00000005583. [Q8CFN5-1]
ENSMUST00000199105; ENSMUSP00000143212; ENSMUSG00000005583. [Q8CFN5-1]
ENSMUST00000199450; ENSMUSP00000143315; ENSMUSG00000005583. [Q8CFN5-2]
GeneIDi17260.
KEGGimmu:17260.
UCSCiuc007rie.2. mouse. [Q8CFN5-4]
uc007rih.2. mouse. [Q8CFN5-5]
uc007rii.3. mouse. [Q8CFN5-3]

Keywords - Coding sequence diversityi

Alternative splicing

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.

Entry informationi

Entry nameiMEF2C_MOUSE
AccessioniPrimary (citable) accession number: Q8CFN5
Secondary accession number(s): Q8R0H1, Q9D7L0, Q9QW20
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: June 7, 2017
This is version 143 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families