CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012396
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myocyte-specific enhancer factor 2D 
Protein Synonyms/Alias
  
Gene Name
 MEF2D 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
64YASTDMDKVLLKYTEubiquitination[1, 2, 3]
68DMDKVLLKYTEYNEPubiquitination[1, 2, 3, 4]
245ANGNSLNKVIPAKSPacetylation[5]
439THPHISIKSEPVSPSacetylation[6]
439THPHISIKSEPVSPSsumoylation[7, 8]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications.
 Zhao X, Sternsdorf T, Bolger TA, Evans RM, Yao TP.
 Mol Cell Biol. 2005 Oct;25(19):8456-64. [PMID: 16166628]
 [7] Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors.
 Grégoire S, Yang XJ.
 Mol Cell Biol. 2005 Mar;25(6):2273-87. [PMID: 15743823]
 [8] Control of MEF2 transcriptional activity by coordinated phosphorylation and sumoylation.
 Grégoire S, Tremblay AM, Xiao L, Yang Q, Ma K, Nie J, Mao Z, Wu Z, Giguère V, Yang XJ.
 J Biol Chem. 2006 Feb 17;281(7):4423-33. [PMID: 16356933
Functional Description
 Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-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). 
Sequence Annotation
 DOMAIN 3 57 MADS-box.
 DNA_BIND 58 86 Mef2-type (Potential).
 REGION 286 292 Beta domain.
 MOD_RES 121 121 Phosphoserine; by PKA.
 MOD_RES 180 180 Phosphoserine; by MAPK7.
 MOD_RES 190 190 Phosphoserine; by PKA (By similarity).
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 245 245 N6-acetyllysine.
 MOD_RES 251 251 Phosphoserine.
 MOD_RES 439 439 N6-acetyllysine; alternate.
 MOD_RES 444 444 Phosphoserine.
 CROSSLNK 439 439 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Activator; Alternative splicing; Apoptosis; Complete proteome; Developmental protein; Differentiation; DNA-binding; Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 521 AA 
Protein Sequence
MGRKKIQIQR ITDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNH SNKLFQYAST 60
DMDKVLLKYT EYNEPHESRT NADIIETLRK KGFNGCDSPE PDGEDSLEQS PLLEDKYRRA 120
SEELDGLFRR YGSTVPAPNF AMPVTVPVSN QSSLQFSNPS GSLVTPSLVT SSLTDPRLLS 180
PQQPALQRNS VSPGLPQRPA SAGAMLGGDL NSANGACPSP VGNGYVSARA SPGLLPVANG 240
NSLNKVIPAK SPPPPTHSTQ LGAPSRKPDL RVITSQAGKG LMHHLTEDHL DLNNAQRLGV 300
SQSTHSLTTP VVSVATPSLL SQGLPFSSMP TAYNTDYQLT SAELSSLPAF SSPGGLSLGN 360
VTAWQQPQQP QQPQQPQPPQ QQPPQPQQPQ PQQPQQPQQP PQQQSHLVPV SLSNLIPGSP 420
LPHVGAALTV TTHPHISIKS EPVSPSRERS PAPPPPAVFP AARPEPGDGL SSPAGGSYET 480
GDRDDGRGDF GPTLGLLRPA PEPEAEGSAV KRMRLDTWTL K 521 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
 GO:0000981; F:sequence-specific DNA binding RNA polymerase II transcription factor activity; IDA:UniProtKB.
 GO:0007512; P:adult heart development; IEP:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0002062; P:chondrocyte differentiation; IEA:Compara.
 GO:0001958; P:endochondral ossification; IEA:Compara.
 GO:0007517; P:muscle organ development; TAS:ProtInc.
 GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
 GO:0001649; P:osteoblast differentiation; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB. 
Interpro
 IPR022102; HJURP_C.
 IPR002100; TF_MADSbox. 
Pfam
 PF12347; HJURP_C
 PF00319; SRF-TF 
SMART
 SM00432; MADS 
PROSITE
 PS00350; MADS_BOX_1
 PS50066; MADS_BOX_2 
PRINTS
 PR00404; MADSDOMAIN.