dbPTM

MEF2D_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MEF2D_MOUSE
UniProt AC	Q63943
Protein Name	Myocyte-specific enhancer factor 2D
Gene Name	Mef2d
Organism	Mus musculus (Mouse).
Sequence Length	514
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..
Protein Sequence	MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSSVPAPNFAMPVTVPVSNQSSMQFSNPSSSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGGDLNSANGACPSPVGNGYVSARASPGLLPVANGNSLNKVIPAKSPPPPTHNTQLGAPSRKPDLRVITSQGGKGLMHHLTEDHLDLNNAQRLGVSQSTHSLTTPVVSVATPSLLSQGLPFSSMPTAYNTDYQLPSAELSSLPAFSSPAGLALGNVTAWQQPQPPQQPQPPQPPQSQPQPPQPQPQQPPQQQPHLVPVSLSNLIPGSPLPHVGAALTVTTHPHISIKSEPVSPSRERSPAPPPPAVFPAARPEPGEGLSSPAGGSYETGDRDDGRGDFGPTLGLLRPAPEPEAEGSAVKRMRLDTWTLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	DERNRQVTFTKRKFG CCHHCCEEEEEHHHC	19.76	15735306
59	Phosphorylation	NKLFQYASTDMDKVL CCHHHHCCCCHHHHH	21.72	8663403
97 (in isoform 2)	Phosphorylation	-	69.49	21183079
98	Phosphorylation	KGFNGCDSPEPDGED CCCCCCCCCCCCCCC	34.93	25521595
106	Phosphorylation	PEPDGEDSLEQSPLL CCCCCCCCCCCCHHH	29.51	24925903
107 (in isoform 2)	Phosphorylation	-	12.27	21183079
110	Phosphorylation	GEDSLEQSPLLEDKY CCCCCCCCHHHHHHH	14.24	24925903
121	Phosphorylation	EDKYRRASEELDGLF HHHHHHHHHHHHHHH	29.77	22942356
180	Phosphorylation	LTDPRLLSPQQPALQ CCCHHHCCCCCCHHH	25.84	27087446
190	Phosphorylation	QPALQRNSVSPGLPQ CCHHHCCCCCCCCCC	26.59	22817900
192	Phosphorylation	ALQRNSVSPGLPQRP HHHCCCCCCCCCCCC	17.05	29472430
201	Phosphorylation	GLPQRPASAGAMLGG CCCCCCCCCCCCCCC	29.89	24759943
212	Phosphorylation	MLGGDLNSANGACPS CCCCCCCCCCCCCCC	30.34	24759943
219	Phosphorylation	SANGACPSPVGNGYV CCCCCCCCCCCCCCE	31.91	24759943
225	Phosphorylation	PSPVGNGYVSARASP CCCCCCCCEECCCCC	8.67	24759943
231	Phosphorylation	GYVSARASPGLLPVA CCEECCCCCCCCCCC	17.59	25521595
242	Phosphorylation	LPVANGNSLNKVIPA CCCCCCCCCCCCCCC	34.42	25619855
245	Acetylation	ANGNSLNKVIPAKSP CCCCCCCCCCCCCCC	47.00	-
251	Phosphorylation	NKVIPAKSPPPPTHN CCCCCCCCCCCCCCC	44.75	26824392
256	Phosphorylation	AKSPPPPTHNTQLGA CCCCCCCCCCCCCCC	33.27	28833060
259	Phosphorylation	PPPPTHNTQLGAPSR CCCCCCCCCCCCCCC	19.98	28833060
286	Phosphorylation	KGLMHHLTEDHLDLN CHHHHHHCHHCCCCC	34.70	29899451
432	Acetylation	THPHISIKSEPVSPS CCCCCEECCCCCCCC	41.81	59823
433	Phosphorylation	HPHISIKSEPVSPSR CCCCEECCCCCCCCC	45.52	21743459
437	Phosphorylation	SIKSEPVSPSRERSP EECCCCCCCCCCCCC	28.07	25521595
439	Phosphorylation	KSEPVSPSRERSPAP CCCCCCCCCCCCCCC	38.99	25521595
443	Phosphorylation	VSPSRERSPAPPPPA CCCCCCCCCCCCCCC	22.21	28066266
464	Phosphorylation	PEPGEGLSSPAGGSY CCCCCCCCCCCCCCC	45.17	25338131
465	Phosphorylation	EPGEGLSSPAGGSYE CCCCCCCCCCCCCCC	24.66	29514104

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
121	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
121	S	Phosphorylation	Kinase	PKACA	P05132	PSP
121	S	Phosphorylation	Kinase	P38A	Q16539	PSP
121	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
121	S	Phosphorylation	Kinase	PKA	-	Uniprot
180	S	Phosphorylation	Kinase	MAPK7	Q13164	GPS
180	S	Phosphorylation	Kinase	MK07	Q9WVS8	PhosphoELM
190	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
190	S	Phosphorylation	Kinase	PKACA	P05132	PSP
190	S	Phosphorylation	Kinase	P38A	Q16539	PSP
190	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
190	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
20	T	Phosphorylation	18299387
No in vitro phosphorylation by PKA on Thr-20.
121	S	Phosphorylation	18299387
Phosphorylated by PKA at Ser-121 and Ser-190 represses transcriptional activity in embryonic and postnatal skeletal muscle, and stabilizes protein levels.
190	S	Phosphorylation	18299387
Phosphorylated by PKA at Ser-121 and Ser-190 represses transcriptional activity in embryonic and postnatal skeletal muscle, and stabilizes protein levels.
432	K	Acetylation	-
Acetylated on Lys-432 by CREBBP.
432	K	Phosphorylation	-
Phosphorylated on Ser-437 is which is required for Lys-432 sumoylation and inhibits transcriptional activity.
432	K	Sumoylation	-
Phosphorylated on Ser-437 is which is required for Lys-432 sumoylation and inhibits transcriptional activity.
432	K	Sumoylation	-
Sumoylated on Lys-432 with SUMO2 but not SUMO1; which inhibits transcriptional activity and myogenic activity.
437	S	Phosphorylation	16407541
Phosphorylated on Ser-437 is which is required for Lys-432 sumoylation and inhibits transcriptional activity.
437	S	Sumoylation	16407541
Phosphorylated on Ser-437 is which is required for Lys-432 sumoylation and inhibits transcriptional activity.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
KDM1A_HUMAN	KDM1A	physical	20833138

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MEF2D_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Protein kinase A represses skeletal myogenesis by targeting myocyteenhancer factor 2D."; Du M., Perry R.L.S., Nowacki N.B., Gordon J.W., Salma J., Zhao J.,Aziz A., Chan J., Siu K.W.M., McDermott J.C.; Mol. Cell. Biol. 28:2952-2970(2008). Cited for: PHOSPHORYLATION AT SER-121 AND SER-190, INTERACTION WITH HDAC4,FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND MUTAGENESIS OFTHR-20; SER-121 AND SER-190.	18299387 [Abstract]
"Calpain-regulated p35/cdk5 plays a central role in dopaminergicneuron death through modulation of the transcription factor myocyteenhancer factor 2."; Smith P.D., Mount M.P., Shree R., Callaghan S., Slack R.S.,Anisman H., Vincent I., Wang X., Mao Z., Park D.S.; J. Neurosci. 26:440-447(2006). Cited for: PHOSPHORYLATION AT SER-437, FUNCTION, TISSUE SPECIFICITY, ANDMUTAGENESIS OF SER-437.	16407541 [Abstract]

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