MEF2D_HUMAN - dbPTM
MEF2D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEF2D_HUMAN
UniProt AC Q14814
Protein Name Myocyte-specific enhancer factor 2D
Gene Name MEF2D
Organism Homo sapiens (Human).
Sequence Length 521
Subcellular Localization Nucleus . Translocated by HDAC4 to nuclear dots.
Protein 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)..
Protein Sequence MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSTVPAPNFAMPVTVPVSNQSSLQFSNPSGSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGGDLNSANGACPSPVGNGYVSARASPGLLPVANGNSLNKVIPAKSPPPPTHSTQLGAPSRKPDLRVITSQAGKGLMHHLTEDHLDLNNAQRLGVSQSTHSLTTPVVSVATPSLLSQGLPFSSMPTAYNTDYQLTSAELSSLPAFSSPGGLSLGNVTAWQQPQQPQQPQQPQPPQQQPPQPQQPQPQQPQQPQQPPQQQSHLVPVSLSNLIPGSPLPHVGAALTVTTHPHISIKSEPVSPSRERSPAPPPPAVFPAARPEPGDGLSSPAGGSYETGDRDDGRGDFGPTLGLLRPAPEPEAEGSAVKRMRLDTWTLK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
23UbiquitinationNRQVTFTKRKFGLMK
HCCEEEEEHHHCCCH		49.7732015554
59PhosphorylationNKLFQYASTDMDKVL
CCHHHHCCCCHHHHH		21.728663403
64 (in isoform 5)Ubiquitination-28.3021890473
64 (in isoform 4)Ubiquitination-28.3021890473
64 (in isoform 3)Ubiquitination-28.3021890473
64 (in isoform 2)Ubiquitination-28.3021890473
64 (in isoform 1)Ubiquitination-28.3021890473
64 (in isoform 6)Ubiquitination-28.3021890473
64UbiquitinationYASTDMDKVLLKYTE
HCCCCHHHHHHHHHH		28.3021890473
68UbiquitinationDMDKVLLKYTEYNEP
CHHHHHHHHHHCCCC		46.0622817900
68 (in isoform 1)Ubiquitination-46.0621890473
68 (in isoform 4)Ubiquitination-46.0621890473
68 (in isoform 3)Ubiquitination-46.0621890473
68 (in isoform 5)Ubiquitination-46.0621890473
68 (in isoform 2)Ubiquitination-46.0621890473
68 (in isoform 6)Ubiquitination-46.0621890473
69PhosphorylationMDKVLLKYTEYNEPH
HHHHHHHHHHCCCCC		12.5526657352
70PhosphorylationDKVLLKYTEYNEPHE
HHHHHHHHHCCCCCC		30.3326657352
78PhosphorylationEYNEPHESRTNADII
HCCCCCCCCCCHHHH		41.1726657352
87PhosphorylationTNADIIETLRKKGFN
CCHHHHHHHHHCCCC		22.8126074081
97 (in isoform 2)Phosphorylation-69.4925954137
97 (in isoform 5)Phosphorylation-69.4925954137
98PhosphorylationKGFNGCDSPEPDGED
CCCCCCCCCCCCCCC		34.9329255136
106PhosphorylationPEPDGEDSLEQSPLL
CCCCCCCCCCCCHHH		29.5130266825
107 (in isoform 2)Phosphorylation-12.2725954137
107 (in isoform 5)Phosphorylation-12.2725954137
110PhosphorylationGEDSLEQSPLLEDKY
CCCCCCCCHHHHHHH		14.2430266825
117PhosphorylationSPLLEDKYRRASEEL
CHHHHHHHHHHHHHH		20.0423927012
121PhosphorylationEDKYRRASEELDGLF
HHHHHHHHHHHHHHH		29.7729255136
180PhosphorylationLTDPRLLSPQQPALQ
CCCHHHCCCCCCHHH		25.8429255136
190PhosphorylationQPALQRNSVSPGLPQ
CCHHHCCCCCCCCCC		26.5923927012
192PhosphorylationALQRNSVSPGLPQRP
HHHCCCCCCCCCCCC		17.0519664994
201PhosphorylationGLPQRPASAGAMLGG
CCCCCCCCCCCCCCC		29.8928450419
212PhosphorylationMLGGDLNSANGACPS
CCCCCCCCCCCCCCC		30.3428450419
219PhosphorylationSANGACPSPVGNGYV
CCCCCCCCCCCCCCE		31.9128450419
227PhosphorylationPVGNGYVSARASPGL
CCCCCCEECCCCCCC		11.98-
231PhosphorylationGYVSARASPGLLPVA
CCEECCCCCCCCCCC		17.5929255136
242PhosphorylationLPVANGNSLNKVIPA
CCCCCCCCCCCCCCC		34.4226055452
245AcetylationANGNSLNKVIPAKSP
CCCCCCCCCCCCCCC		47.0019608861
250UbiquitinationLNKVIPAKSPPPPTH
CCCCCCCCCCCCCCC		59.1329967540
250AcetylationLNKVIPAKSPPPPTH
CCCCCCCCCCCCCCC		59.1325953088
251PhosphorylationNKVIPAKSPPPPTHS
CCCCCCCCCCCCCCC		44.7529255136
256PhosphorylationAKSPPPPTHSTQLGA
CCCCCCCCCCCCCCC		33.9422167270
258PhosphorylationSPPPPTHSTQLGAPS
CCCCCCCCCCCCCCC		21.9622167270
259PhosphorylationPPPPTHSTQLGAPSR
CCCCCCCCCCCCCCC		21.8722167270
265PhosphorylationSTQLGAPSRKPDLRV
CCCCCCCCCCCCCEE		53.0223403867
267MethylationQLGAPSRKPDLRVIT
CCCCCCCCCCCEEEE		47.42-
267"N6,N6-dimethyllysine"QLGAPSRKPDLRVIT
CCCCCCCCCCCEEEE		47.42-
275O-linked_GlycosylationPDLRVITSQAGKGLM
CCCEEEECCCCCHHH		13.6020068230
275O-linked_GlycosylationPDLRVITSQAGKGLM
CCCEEEECCCCCHHH		13.6029406951
286PhosphorylationKGLMHHLTEDHLDLN
CHHHHHHCHHCCCCC		34.7024719451
437PhosphorylationVTTHPHISIKSEPVS
EECCCCCEECCCCCC		22.4124719451
439SumoylationTHPHISIKSEPVSPS
CCCCCEECCCCCCCC		41.81-
439SumoylationTHPHISIKSEPVSPS
CCCCCEECCCCCCCC		41.8116166628
439AcetylationTHPHISIKSEPVSPS
CCCCCEECCCCCCCC		41.8116166628
440PhosphorylationHPHISIKSEPVSPSR
CCCCEECCCCCCCCC		45.5223403867
444PhosphorylationSIKSEPVSPSRERSP
EECCCCCCCCCCCCC		28.0715888658
446PhosphorylationKSEPVSPSRERSPAP
CCCCCCCCCCCCCCC		38.9930266825
450PhosphorylationVSPSRERSPAPPPPA
CCCCCCCCCCCCCCC		22.2123401153
465PhosphorylationVFPAARPEPGDGLSS
CCCCCCCCCCCCCCC		57.2632142685
471PhosphorylationPEPGDGLSSPAGGSY
CCCCCCCCCCCCCCC		39.5423401153
472PhosphorylationEPGDGLSSPAGGSYE
CCCCCCCCCCCCCCC		24.6629255136
477PhosphorylationLSSPAGGSYETGDRD
CCCCCCCCCCCCCCC		20.9123663014
478PhosphorylationSSPAGGSYETGDRDD
CCCCCCCCCCCCCCC		22.3023663014
480PhosphorylationPAGGSYETGDRDDGR
CCCCCCCCCCCCCCC		35.8330108239
508PhosphorylationPEPEAEGSAVKRMRL
CCCCCCCCCCEEEEC		22.7625159151
511AcetylationEAEGSAVKRMRLDTW
CCCCCCCEEEECCCE		39.9523954790
517PhosphorylationVKRMRLDTWTLK---
CEEEECCCEECC---		25.5818212344
521AcetylationRLDTWTLK-------
ECCCEECC-------		51.4269159
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
98SPhosphorylationKinaseCDK4P11802
PSP
110SPhosphorylationKinaseCDK4P11802
PSP
121SPhosphorylationKinasePKA-FAMILY-GPS
121SPhosphorylationKinasePKA-Uniprot
180SPhosphorylationKinaseMAPK7Q13164
Uniprot
190SPhosphorylationKinasePKA-Uniprot
444SPhosphorylationKinaseCDK5Q00535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
180SPhosphorylation

10849446
439KAcetylation

15743823
439KPhosphorylation

15743823
439KSumoylation

15743823
439KSumoylation

15743823
444SPhosphorylation

12691662
444SSumoylation

12691662
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MEF2D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433T_HUMANYWHAQphysical
11433030
HDAC5_HUMANHDAC5physical
12896970
EP300_HUMANEP300physical
10825153
CABIN_HUMANCABIN1physical
10933397
EP300_HUMANEP300physical
10933397
CABIN_HUMANCABIN1physical
10531067
NFAC2_HUMANNFATC2physical
10944115
MEF2A_HUMANMEF2Aphysical
8798771
CSN5_HUMANCOPS5physical
20936779
HDAC3_HUMANHDAC3physical
17158926
HDAC4_HUMANHDAC4physical
17158926
HDAC4_HUMANHDAC4physical
16166628
SENP3_HUMANSENP3physical
15743823
ASH2L_HUMANASH2Lphysical
18026121
MEN1_HUMANMEN1physical
18026121
RBBP5_HUMANRBBP5physical
18026121
KMT2D_HUMANKMT2Dphysical
18026121
MEF2A_HUMANMEF2Aphysical
20590529
HDAC1_HUMANHDAC1physical
20590529
CABIN_HUMANCABIN1physical
15902271
A4_HUMANAPPphysical
21832049
SKP2_HUMANSKP2physical
25733682
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MEF2D_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, AND MASS SPECTROMETRY.
"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).
Cited for: SUMOYLATION AT LYS-439, ACETYLATION AT LYS-439, DEACETYLATION, ANDMUTAGENESIS OF ILE-438 AND LYS-439.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-106; SER-110;SER-121; SER-180; SER-231 AND SER-251, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND MASSSPECTROMETRY.
"Control of MEF2 transcriptional activity by coordinatedphosphorylation 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).
Cited for: SUMOYLATION AT LYS-439, PHOSPHORYLATION AT SER-444, AND MUTAGENESIS OFLYS-439 AND SER-444.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-106 AND SER-110,AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASSSPECTROMETRY.
"Cdk5-mediated inhibition of the protective effects of transcriptionfactor 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).
Cited for: PHOSPHORYLATION AT SER-444, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-444.
"Big mitogen-activated kinase regulates multiple members of the MEF2protein 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).
Cited for: PHOSPHORYLATION AT SER-180, FUNCTION, AND MUTAGENESIS OF SER-180 ANDSER-437.
Sumoylation
ReferencePubMed
"Control of MEF2 transcriptional activity by coordinatedphosphorylation 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).
Cited for: SUMOYLATION AT LYS-439, PHOSPHORYLATION AT SER-444, AND MUTAGENESIS OFLYS-439 AND SER-444.
"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).
Cited for: SUMOYLATION AT LYS-439, ACETYLATION AT LYS-439, DEACETYLATION, ANDMUTAGENESIS OF ILE-438 AND LYS-439.
"Association with class IIa histone deacetylases upregulates thesumoylation of MEF2 transcription factors.";
Gregoire S., Yang X.-J.;
Mol. Cell. Biol. 25:2273-2287(2005).
Cited for: SUMOYLATION AT LYS-439, SUBCELLULAR LOCATION, AND FUNCTION.

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