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Q14814

- MEF2D_HUMAN

UniProt

Q14814 - MEF2D_HUMAN

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Protein
Myocyte-specific enhancer factor 2D
Gene
MEF2D
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei288 – 2892Cleavage Inferred

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi58 – 8629Mef2-type Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  2. activating transcription factor binding Source: UniProtKB
  3. histone deacetylase binding Source: UniProtKB
  4. protein binding Source: BHF-UCL
  5. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  6. sequence-specific DNA binding transcription factor activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. adult heart development Source: UniProtKB
  2. apoptotic process Source: UniProtKB-KW
  3. chondrocyte differentiation Source: Ensembl
  4. endochondral ossification Source: Ensembl
  5. muscle organ development Source: ProtInc
  6. nervous system development Source: UniProtKB-KW
  7. osteoblast differentiation Source: Ensembl
  8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  9. skeletal muscle cell differentiation Source: Ensembl
  10. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_21402. CDO in myogenesis.
REACT_24941. Circadian Clock.
SignaLinkiQ14814.

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2D
Gene namesi
Name:MEF2D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6997. MEF2D.

Subcellular locationi

Nucleus
Note: Translocated by HDAC4 to nuclear dots.2 Publications

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi180 – 1801S → A: Abolishes MAPK7- and EGF-mediated transcriptional activation. 1 Publication
Mutagenesisi286 – 2861T → A: Same transcriptional activity as for isoforms with beta domain. 1 Publication
Mutagenesisi287 – 2871E → Q: Abolishes transcriptional activity; when associated with N-288 and N-291. 1 Publication
Mutagenesisi288 – 2881D → A: Abolishes cleavage by caspase 7. 2 Publications
Mutagenesisi288 – 2881D → N: Abolishes transcriptional activity; when associated with Q-287 and N-291. 2 Publications
Mutagenesisi289 – 2891H → A: Same transcriptional activity as for isoforms with beta domain. 1 Publication
Mutagenesisi291 – 2911D → N: Abolishes transcriptional activity; when associated with Q-287 and N-288. 1 Publication
Mutagenesisi437 – 4371S → A: No effect on MAPK7- or EGF-mediated transcriptional activity. 1 Publication
Mutagenesisi438 – 4381I → A: Abolishes K-439 sumoylation. 1 Publication
Mutagenesisi439 – 4391K → R: Abolishes sumoylation and acetylation. 2 Publications
Mutagenesisi444 – 4441S → A: Abolishes K-439 sumoylation. Reduced neurotoxin-induced apoptosis of neuronal cells. More resistant to degradation. 3 Publications
Mutagenesisi444 – 4441S → E: No effect on K-439 sumoylation. 3 Publications

Organism-specific databases

PharmGKBiPA30735.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Myocyte-specific enhancer factor 2D
PRO_0000199435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211Phosphoserine; by PKA
Modified residuei180 – 1801Phosphoserine; by MAPK74 Publications
Modified residuei190 – 1901Phosphoserine; by PKA By similarity
Modified residuei231 – 2311Phosphoserine1 Publication
Modified residuei245 – 2451N6-acetyllysine1 Publication
Modified residuei251 – 2511Phosphoserine1 Publication
Modified residuei439 – 4391N6-acetyllysine; alternate1 Publication
Cross-linki439 – 439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate3 Publications
Modified residuei444 – 4441Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated on Ser-444 by CDK5 is required for Lys-439 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 CaMK4.5 Publications
Acetylated on Lys-439 by CREBBP. Deacetylated by SIRT1.2 Publications
Sumoylated on Lys-439 with SUMO2 but not SUMO1; which inhibits transcriptional activity and myogenic activity. Desumoylated by SENP3.3 Publications
Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation By similarity.5 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14814.
PaxDbiQ14814.
PRIDEiQ14814.

PTM databases

PhosphoSiteiQ14814.

Miscellaneous databases

PMAP-CutDBQ14814.

Expressioni

Developmental stagei

Present in myotubes and also in undifferentiated myoblasts.

Gene expression databases

ArrayExpressiQ14814.
BgeeiQ14814.
CleanExiHS_MEF2D.
GenevestigatoriQ14814.

Organism-specific databases

HPAiHPA004807.
HPA007114.

Interactioni

Subunit structurei

Interacts with MYOG By similarity. 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. Forms a heterodimer with MEF2A.2 Publications

Protein-protein interaction databases

BioGridi110373. 31 interactions.
IntActiQ14814. 8 interactions.
MINTiMINT-125484.
STRINGi9606.ENSP00000271555.

Structurei

3D structure databases

ProteinModelPortaliQ14814.
SMRiQ14814. Positions 2-73.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 5755MADS-box
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 2927Beta domain

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 3129Arg/Lys-rich (basic)
Add
BLAST
Compositional biasi252 – 2554Poly-Pro
Compositional biasi365 – 40440Gln/Pro-rich
Add
BLAST
Compositional biasi451 – 4566Poly-Pro

Domaini

The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity.1 Publication

Sequence similaritiesi

Belongs to the MEF2 family.
Contains 1 MADS-box domain.

Phylogenomic databases

eggNOGiCOG5068.
HOVERGENiHBG053944.
InParanoidiQ14814.
KOiK09262.
OMAiHHLNNAQ.
OrthoDBiEOG793B7D.
PhylomeDBiQ14814.
TreeFamiTF314067.

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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform MEF2DAB (identifier: Q14814-1) [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

MGRKKIQIQR ITDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNH    50
SNKLFQYAST DMDKVLLKYT EYNEPHESRT NADIIETLRK KGFNGCDSPE 100
PDGEDSLEQS PLLEDKYRRA SEELDGLFRR YGSTVPAPNF AMPVTVPVSN 150
QSSLQFSNPS GSLVTPSLVT SSLTDPRLLS PQQPALQRNS VSPGLPQRPA 200
SAGAMLGGDL NSANGACPSP VGNGYVSARA SPGLLPVANG NSLNKVIPAK 250
SPPPPTHSTQ LGAPSRKPDL RVITSQAGKG LMHHLTEDHL DLNNAQRLGV 300
SQSTHSLTTP VVSVATPSLL SQGLPFSSMP TAYNTDYQLT SAELSSLPAF 350
SSPGGLSLGN VTAWQQPQQP QQPQQPQPPQ QQPPQPQQPQ PQQPQQPQQP 400
PQQQSHLVPV SLSNLIPGSP LPHVGAALTV TTHPHISIKS EPVSPSRERS 450
PAPPPPAVFP AARPEPGDGL SSPAGGSYET GDRDDGRGDF GPTLGLLRPA 500
PEPEAEGSAV KRMRLDTWTL K 521
Length:521
Mass (Da):55,938
Last modified:November 1, 1997 - v1
Checksum:i5C9790AD598619BA
GO
Isoform MEF2DA'B (identifier: Q14814-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: TLRKKGFNGC...ELDGLFRRYG → ALHKKHRECE...DKMMQSYRLA

Show »
Length:520
Mass (Da):56,091
Checksum:i9B39CB2A3570EB74
GO
Isoform MEF2D0B (identifier: Q14814-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: Missing.

Show »
Length:475
Mass (Da):50,680
Checksum:iBCA6D1EF6885A467
GO
Isoform MEF2DA0 (identifier: Q14814-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     286-292: Missing.

Show »
Length:514
Mass (Da):55,114
Checksum:i425430A7A0F69549
GO
Isoform MEF2DA'0 (identifier: Q14814-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: TLRKKGFNGC...ELDGLFRRYG → ALHKKHRECE...DKMMQSYRLA
     286-292: Missing.

Show »
Length:513
Mass (Da):55,267
Checksum:i2CC3FD705A1C8D1F
GO
Isoform MEF2D00 (identifier: Q14814-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: Missing.
     286-292: Missing.

Show »
Length:468
Mass (Da):49,856
Checksum:iBFFEBF282D6519F7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti434 – 4341P → S.
Corresponds to variant rs2274315 [ dbSNP | Ensembl ].
VAR_022155

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei87 – 13246Missing in isoform MEF2D0B and isoform MEF2D00.
VSP_006251Add
BLAST
Alternative sequencei87 – 13246TLRKK…FRRYG → ALHKKHRECESPEVDEVFAL TPQTEEKYKKIDEEFDKMMQ SYRLA in isoform MEF2DA'B and isoform MEF2DA'0.
VSP_006250Add
BLAST
Alternative sequencei286 – 2927Missing in isoform MEF2DA0, isoform MEF2DA'0 and isoform MEF2D00.
VSP_006252

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L16794 mRNA. Translation: AAA93194.1.
L16795 Genomic DNA. Translation: AAA59579.1.
AL139412 Genomic DNA. Translation: CAI17184.1.
AL139412 Genomic DNA. Translation: CAI17185.1.
CH471121 Genomic DNA. Translation: EAW52948.1.
CH471121 Genomic DNA. Translation: EAW52952.1.
BC040949 mRNA. Translation: AAH40949.1.
BC054520 mRNA. Translation: AAH54520.1.
CCDSiCCDS1143.1. [Q14814-1]
CCDS60304.1. [Q14814-4]
PIRiI53124.
RefSeqiNP_001258558.1. NM_001271629.1. [Q14814-4]
NP_005911.1. NM_005920.3. [Q14814-1]
XP_005245226.1. XM_005245169.2. [Q14814-1]
XP_005245227.1. XM_005245170.1. [Q14814-1]
XP_006711393.1. XM_006711330.1. [Q14814-1]
XP_006711394.1. XM_006711331.1. [Q14814-1]
XP_006711395.1. XM_006711332.1. [Q14814-2]
XP_006711396.1. XM_006711333.1. [Q14814-4]
XP_006711397.1. XM_006711334.1. [Q14814-5]
UniGeneiHs.314327.
Hs.744524.

Genome annotation databases

EnsembliENST00000340875; ENSP00000343159; ENSG00000116604. [Q14814-2]
ENST00000348159; ENSP00000271555; ENSG00000116604. [Q14814-1]
ENST00000353795; ENSP00000344705; ENSG00000116604. [Q14814-3]
ENST00000360595; ENSP00000353803; ENSG00000116604. [Q14814-4]
ENST00000368240; ENSP00000357223; ENSG00000116604. [Q14814-4]
ENST00000464356; ENSP00000476788; ENSG00000116604. [Q14814-5]
GeneIDi4209.
KEGGihsa:4209.
UCSCiuc001fpb.4. human. [Q14814-4]
uc001fpc.4. human. [Q14814-1]

Polymorphism databases

DMDMi2500876.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L16794 mRNA. Translation: AAA93194.1 .
L16795 Genomic DNA. Translation: AAA59579.1 .
AL139412 Genomic DNA. Translation: CAI17184.1 .
AL139412 Genomic DNA. Translation: CAI17185.1 .
CH471121 Genomic DNA. Translation: EAW52948.1 .
CH471121 Genomic DNA. Translation: EAW52952.1 .
BC040949 mRNA. Translation: AAH40949.1 .
BC054520 mRNA. Translation: AAH54520.1 .
CCDSi CCDS1143.1. [Q14814-1 ]
CCDS60304.1. [Q14814-4 ]
PIRi I53124.
RefSeqi NP_001258558.1. NM_001271629.1. [Q14814-4 ]
NP_005911.1. NM_005920.3. [Q14814-1 ]
XP_005245226.1. XM_005245169.2. [Q14814-1 ]
XP_005245227.1. XM_005245170.1. [Q14814-1 ]
XP_006711393.1. XM_006711330.1. [Q14814-1 ]
XP_006711394.1. XM_006711331.1. [Q14814-1 ]
XP_006711395.1. XM_006711332.1. [Q14814-2 ]
XP_006711396.1. XM_006711333.1. [Q14814-4 ]
XP_006711397.1. XM_006711334.1. [Q14814-5 ]
UniGenei Hs.314327.
Hs.744524.

3D structure databases

ProteinModelPortali Q14814.
SMRi Q14814. Positions 2-73.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110373. 31 interactions.
IntActi Q14814. 8 interactions.
MINTi MINT-125484.
STRINGi 9606.ENSP00000271555.

PTM databases

PhosphoSitei Q14814.

Polymorphism databases

DMDMi 2500876.

Proteomic databases

MaxQBi Q14814.
PaxDbi Q14814.
PRIDEi Q14814.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340875 ; ENSP00000343159 ; ENSG00000116604 . [Q14814-2 ]
ENST00000348159 ; ENSP00000271555 ; ENSG00000116604 . [Q14814-1 ]
ENST00000353795 ; ENSP00000344705 ; ENSG00000116604 . [Q14814-3 ]
ENST00000360595 ; ENSP00000353803 ; ENSG00000116604 . [Q14814-4 ]
ENST00000368240 ; ENSP00000357223 ; ENSG00000116604 . [Q14814-4 ]
ENST00000464356 ; ENSP00000476788 ; ENSG00000116604 . [Q14814-5 ]
GeneIDi 4209.
KEGGi hsa:4209.
UCSCi uc001fpb.4. human. [Q14814-4 ]
uc001fpc.4. human. [Q14814-1 ]

Organism-specific databases

CTDi 4209.
GeneCardsi GC01M156433.
HGNCi HGNC:6997. MEF2D.
HPAi HPA004807.
HPA007114.
MIMi 600663. gene.
neXtProti NX_Q14814.
PharmGKBi PA30735.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5068.
HOVERGENi HBG053944.
InParanoidi Q14814.
KOi K09262.
OMAi HHLNNAQ.
OrthoDBi EOG793B7D.
PhylomeDBi Q14814.
TreeFami TF314067.

Enzyme and pathway databases

Reactomei REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_21402. CDO in myogenesis.
REACT_24941. Circadian Clock.
SignaLinki Q14814.

Miscellaneous databases

ChiTaRSi MEF2D. human.
GeneWikii MEF2D.
GenomeRNAii 4209.
NextBioi 16582.
PMAP-CutDB Q14814.
PROi Q14814.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14814.
Bgeei Q14814.
CleanExi HS_MEF2D.
Genevestigatori Q14814.

Family and domain databases

InterProi IPR022102. HJURP_C.
IPR002100. TF_MADSbox.
[Graphical view ]
Pfami PF12347. HJURP_C. 1 hit.
PF00319. SRF-TF. 1 hit.
[Graphical view ]
PRINTSi PR00404. MADSDOMAIN.
SMARTi SM00432. MADS. 1 hit.
[Graphical view ]
SUPFAMi SSF55455. SSF55455. 1 hit.
PROSITEi PS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage."
    Breitbart R.E., Liang C.-S., Smoot L.B., Laheru D.A., Mahdavi V., Nadal-Ginard B.
    Development 118:1095-1106(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS MEF2D00; MEF2D0B; MEF2DA'0; MEF2DA'B; MEF2DA0 AND MEF2DAB).
    Tissue: Myocardium.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 MEF2DA0 AND MEF2DAB).
    Tissue: Eye and Testis.
  5. "Regulation of the MEF2 family of transcription factors by p38."
    Zhao M., New L., Kravchenko V.V., Kato Y., Gram H., di Padova F., Olson E.N., Ulevitch R.J., Han J.-D.
    Mol. Cell. Biol. 19:21-30(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: HETERODIMERIZATION.
  6. "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor."
    Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., Th'ng J., Han J., Yang X.-J.
    Mol. Cell. Biol. 19:7816-7827(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC4.
  7. "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family."
    Kato Y., Zhao M., Morikawa A., Sugiyama T., Chakravortty D., Koide N., Yoshida T., Tapping R.I., Yang Y., Yokochi T., Lee J.D.
    J. Biol. Chem. 275:18534-18540(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-180, FUNCTION, MUTAGENESIS OF SER-180 AND SER-437.
  8. "Ca(2+)-dependent gene expression mediated by MEF2 transcription factors."
    Blaeser F., Ho N., Prywes R., Chatila T.A.
    J. Biol. Chem. 275:197-209(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CAMK4.
  9. "Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis."
    Okamoto S., Li Z., Ju C., Scholzke M.N., Mathews E., Cui J., Salvesen G.S., Bossy-Wetzel E., Lipton S.A.
    Proc. Natl. Acad. Sci. U.S.A. 99:3974-3979(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING AT ASP-288, FUNCTION, MUTAGENESIS OF ASP-288.
  10. "Cdk5-mediated inhibition of the protective effects of transcription factor MEF2 in neurotoxicity-induced apoptosis."
    Gong X., Tang X., Wiedmann M., Wang X., Peng J., Zheng D., Blair L.A.C., Marshall J., Mao Z.
    Neuron 38:33-46(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-444, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-444.
  11. "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: FUNCTION OF BETA DOMAIN, MUTAGENESIS OF THR-286; GLU-287; ASP-288; HIS-289 AND ASP-291.
  12. "Cyclin-dependent kinase 5 mediates neurotoxin-induced degradation of the transcription factor myocyte enhancer factor 2."
    Tang X., Wang X., Gong X., Tong M., Park D., Xia Z., Mao Z.
    J. Neurosci. 25:4823-4834(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, PHOSPHORYLATION AT SER-444, MUTAGENESIS OF SER-444.
  13. "Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors."
    Gregoire S., Yang X.-J.
    Mol. Cell. Biol. 25:2273-2287(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-439, SUBCELLULAR LOCATION, FUNCTION.
  14. "Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications."
    Zhao X., Sternsdorf T., Bolger T.A., Evans R.M., Yao T.-P.
    Mol. Cell. Biol. 25:8456-8464(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-439, ACETYLATION AT LYS-439, DEACETYLATION, MUTAGENESIS OF ILE-438 AND LYS-439.
  15. "Myocyte enhancer factor 2 acetylation by p300 enhances its DNA binding activity, transcriptional activity, and myogenic differentiation."
    Ma K., Chan J.K., Zhu G., Wu Z.
    Mol. Cell. Biol. 25:3575-3582(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION.
  16. "Control of MEF2 transcriptional activity by coordinated phosphorylation and sumoylation."
    Gregoire S., Tremblay A.M., Xiao L., Yang Q., Ma K., Nie J., Mao Z., Wu Z., Giguere V., Yang X.-J.
    J. Biol. Chem. 281:4423-4433(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-439, PHOSPHORYLATION AT SER-444, MUTAGENESIS OF LYS-439 AND SER-444.
  17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMEF2D_HUMAN
AccessioniPrimary (citable) accession number: Q14814
Secondary accession number(s): D3DVC0
, Q14815, Q5T9U5, Q5T9U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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