dbPTM

MEF2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MEF2A_HUMAN
UniProt AC	Q02078
Protein Name	Myocyte-specific enhancer factor 2A
Gene Name	MEF2A
Organism	Homo sapiens (Human).
Sequence Length	507
Subcellular Localization	Nucleus .
Protein Description	Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous 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. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter..
Protein Sequence	MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGFVNSRASPNLIGATGANSLGKVMPTKSPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30 (in isoform 7)	Phosphorylation	-	39.02	30266825
30 (in isoform 8)	Phosphorylation	-	39.02	30266825
36 (in isoform 7)	Phosphorylation	-	10.91	26657352
36 (in isoform 8)	Phosphorylation	-	10.91	26657352
40 (in isoform 7)	Phosphorylation	-	28.99	23927012
40 (in isoform 8)	Phosphorylation	-	28.99	23927012
43 (in isoform 7)	Phosphorylation	-	4.80	28450419
43 (in isoform 8)	Phosphorylation	-	4.80	28450419
48 (in isoform 7)	Phosphorylation	-	6.02	22199227
48 (in isoform 8)	Phosphorylation	-	6.02	22199227
59	Phosphorylation	NKLFQYASTDMDKVL CCHHHCCCCCHHHHH	21.72	15979805
59	Ubiquitination	NKLFQYASTDMDKVL CCHHHCCCCCHHHHH	21.72	21890473
59	Ubiquitination	NKLFQYASTDMDKVL CCHHHCCCCCHHHHH	21.72	21890473
64	Ubiquitination	YASTDMDKVLLKYTE CCCCCHHHHHHHHHC	28.30	-
64 (in isoform 1)	Ubiquitination	-	28.30	21890473
64 (in isoform 2)	Ubiquitination	-	28.30	21890473
64 (in isoform 3)	Ubiquitination	-	28.30	21890473
64 (in isoform 4)	Ubiquitination	-	28.30	21890473
64 (in isoform 5)	Ubiquitination	-	28.30	21890473
64	Ubiquitination	YASTDMDKVLLKYTE CCCCCHHHHHHHHHC	28.30	21890473
68	Ubiquitination	DMDKVLLKYTEYNEP CHHHHHHHHHCCCCC	46.06	-
68 (in isoform 1)	Ubiquitination	-	46.06	21890473
68 (in isoform 2)	Ubiquitination	-	46.06	21890473
68 (in isoform 3)	Ubiquitination	-	46.06	21890473
68 (in isoform 4)	Ubiquitination	-	46.06	21890473
68 (in isoform 5)	Ubiquitination	-	46.06	21890473
68	Ubiquitination	DMDKVLLKYTEYNEP CHHHHHHHHHCCCCC	46.06	21890473
69	Phosphorylation	MDKVLLKYTEYNEPH HHHHHHHHHCCCCCC	12.55	26657352
70	Phosphorylation	DKVLLKYTEYNEPHE HHHHHHHHCCCCCCC	30.33	26657352
78	Phosphorylation	EYNEPHESRTNSDIV CCCCCCCCCCCHHHH	41.17	26657352
98	Phosphorylation	KEHRGCDSPDPDTSY HHHCCCCCCCCCCCC	34.97	22167270
98 (in isoform 2)	Phosphorylation	-	34.97	30266825
98 (in isoform 4)	Phosphorylation	-	34.97	30266825
98 (in isoform 6)	Phosphorylation	-	34.97	30266825
103	Phosphorylation	CDSPDPDTSYVLTPH CCCCCCCCCCEECCC	27.61	30266825
104	Phosphorylation	DSPDPDTSYVLTPHT CCCCCCCCCEECCCC	22.18	23927012
104 (in isoform 2)	Phosphorylation	-	22.18	26657352
104 (in isoform 4)	Phosphorylation	-	22.18	26657352
104 (in isoform 6)	Phosphorylation	-	22.18	26657352
105	Phosphorylation	SPDPDTSYVLTPHTE CCCCCCCCEECCCCH	11.11	23927012
108	Phosphorylation	PDTSYVLTPHTEEKY CCCCCEECCCCHHHH	11.72	23927012
108 (in isoform 2)	Phosphorylation	-	11.72	23927012
108 (in isoform 4)	Phosphorylation	-	11.72	23927012
108 (in isoform 6)	Phosphorylation	-	11.72	23927012
111	Phosphorylation	SYVLTPHTEEKYKKI CCEECCCCHHHHHHH	47.22	23927012
111 (in isoform 2)	Phosphorylation	-	47.22	28450419
111 (in isoform 4)	Phosphorylation	-	47.22	28450419
111 (in isoform 6)	Phosphorylation	-	47.22	28450419
115	Phosphorylation	TPHTEEKYKKINEEF CCCCHHHHHHHHHHH	22.31	23312004
116 (in isoform 2)	Phosphorylation	-	59.24	22199227
116 (in isoform 4)	Phosphorylation	-	59.24	22199227
116 (in isoform 6)	Phosphorylation	-	59.24	22199227
127 (in isoform 2)	Ubiquitination	-	31.19	21890473
127 (in isoform 4)	Ubiquitination	-	31.19	21890473
127	Ubiquitination	EEFDNMMRNHKIAPG HHHHHHHHHCCCCCC	31.19	21890473
177	Phosphorylation	ASSTLTDSSMLSPPQ CCCCCCCHHCCCCCC	16.65	26074081
178	Phosphorylation	SSTLTDSSMLSPPQT CCCCCCHHCCCCCCC	26.93	26074081
181	Phosphorylation	LTDSSMLSPPQTTLH CCCHHCCCCCCCEEC	26.37	26074081
185	Phosphorylation	SMLSPPQTTLHRNVS HCCCCCCCEECCCCC	36.78	26074081
186	Phosphorylation	MLSPPQTTLHRNVSP CCCCCCCEECCCCCC	18.47	26074081
192	Phosphorylation	TTLHRNVSPGAPQRP CEECCCCCCCCCCCC	22.59	26074081
201	Phosphorylation	GAPQRPPSTGNAGGM CCCCCCCCCCCCCCC	52.18	26074081
202	Phosphorylation	APQRPPSTGNAGGML CCCCCCCCCCCCCCE	39.98	26074081
210	Phosphorylation	GNAGGMLSTTDLTVP CCCCCCEEECCEECC	21.99	26074081
211	Phosphorylation	NAGGMLSTTDLTVPN CCCCCEEECCEECCC	21.99	26074081
212	Phosphorylation	AGGMLSTTDLTVPNG CCCCEEECCEECCCC	26.15	26074081
215	Phosphorylation	MLSTTDLTVPNGAGS CEEECCEECCCCCCC	36.41	25247763
223	Phosphorylation	VPNGAGSSPVGNGFV CCCCCCCCCCCCCCC	23.76	25921289
235	Phosphorylation	GFVNSRASPNLIGAT CCCCCCCCCCCCCCC	17.14	29255136
246	Phosphorylation	IGATGANSLGKVMPT CCCCCCCCCCCCCCC	37.65	28555341
249	Acetylation	TGANSLGKVMPTKSP CCCCCCCCCCCCCCC	40.42	19608861
253	Phosphorylation	SLGKVMPTKSPPPPG CCCCCCCCCCCCCCC	26.51	23927012
255	Phosphorylation	GKVMPTKSPPPPGGG CCCCCCCCCCCCCCC	45.15	29255136
268	Phosphorylation	GGNLGMNSRKPDLRV CCCCCCCCCCCCEEE	32.56	23403867
280	O-linked_Glycosylation	LRVVIPPSSKGMMPP EEEECCCCCCCCCCC	39.05	30059200
281	O-linked_Glycosylation	RVVIPPSSKGMMPPL EEECCCCCCCCCCCC	38.72	30059200
289	Phosphorylation	KGMMPPLSEEEELEL CCCCCCCCHHHHHHH	49.05	12586839
304	Phosphorylation	NTQRISSSQATQPLA HHEECCCCCCCCCCC	19.62	9858528
311	Phosphorylation	SQATQPLATPVVSVT CCCCCCCCCCEEEEE	19.28	9858528
312	Phosphorylation	QATQPLATPVVSVTT CCCCCCCCCEEEEEC	25.05	9858528
319	Phosphorylation	TPVVSVTTPSLPPQG CCEEEEECCCCCCCC	14.55	9858528
347	Phosphorylation	YSLTSADLSALQGFN CCCCHHHHHHHCCCC	3.01	10849446
355	Phosphorylation	SALQGFNSPGMLSLG HHHCCCCCCCCEEHH	22.14	10849446
400	Phosphorylation	SINTNQNISIKSEPI EEECCCCCEEECCCC	3.03	12691662
401	Phosphorylation	INTNQNISIKSEPIS EECCCCCEEECCCCC	31.36	24719451
403	Acetylation	TNQNISIKSEPISPP CCCCCEEECCCCCCC	41.81	16484498
403	Sumoylation	TNQNISIKSEPISPP CCCCCEEECCCCCCC	41.81	-
403	Sumoylation	TNQNISIKSEPISPP CCCCCEEECCCCCCC	41.81	-
404	Phosphorylation	NQNISIKSEPISPPR CCCCEEECCCCCCCC	47.11	23403867
408	Phosphorylation	SIKSEPISPPRDRMT EEECCCCCCCCCCCC	39.30	23401153
415	Phosphorylation	SPPRDRMTPSGFQQQ CCCCCCCCCCHHHHH	18.39	28348404
417	Phosphorylation	PRDRMTPSGFQQQQQ CCCCCCCCHHHHHHH	42.97	28348404
445	Phosphorylation	QPQPPQPQPRQEMGR CCCCCCCCCCCCCCC	40.33	9858528
453	Phosphorylation	PRQEMGRSPVDSLSS CCCCCCCCCCHHHCC	24.44	9858528
457	Phosphorylation	MGRSPVDSLSSSSSS CCCCCCHHHCCCCCC	30.31	27732954
459	Phosphorylation	RSPVDSLSSSSSSYD CCCCHHHCCCCCCCC	31.93	23312004
460	Phosphorylation	SPVDSLSSSSSSYDG CCCHHHCCCCCCCCC	39.26	22210691
462	Phosphorylation	VDSLSSSSSSYDGSD CHHHCCCCCCCCCCC	25.83	22210691
463	Phosphorylation	DSLSSSSSSYDGSDR HHHCCCCCCCCCCCC	34.56	22210691
465	Phosphorylation	LSSSSSSYDGSDRED HCCCCCCCCCCCCCC	26.69	22210691
468	Phosphorylation	SSSSYDGSDREDPRG CCCCCCCCCCCCCCC	30.51	22210691
479	Phosphorylation	DPRGDFHSPIVLGRP CCCCCCCCCCCCCCC	19.13	23401153
488	Phosphorylation	IVLGRPPNTEDRESP CCCCCCCCCCCCCCC	59.80	20068231
489	Phosphorylation	VLGRPPNTEDRESPS CCCCCCCCCCCCCCC	45.07	26055452
494	Phosphorylation	PNTEDRESPSVKRMR CCCCCCCCCCHHHCC	24.30	25159151
496	Phosphorylation	TEDRESPSVKRMRMD CCCCCCCCHHHCCCE	49.93	25022875
498	Acetylation	DRESPSVKRMRMDAW CCCCCCHHHCCCEEC	44.83	25953088

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
59	S	Phosphorylation	Kinase	CK2	-	Uniprot
98	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
108	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
192	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
223	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
255	S	Phosphorylation	Kinase	MAPK14	Q16539	Uniprot
289	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
312	T	Phosphorylation	Kinase	MAPK7	Q13164	GPS
312	T	Phosphorylation	Kinase	P38-SUBFAMILY	-	GPS
312	T	Phosphorylation	Kinase	NLK	Q9UBE8	Uniprot
312	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
319	T	Phosphorylation	Kinase	MK07	Q13164	PhosphoELM
319	T	Phosphorylation	Kinase	P38-SUBFAMILY	-	GPS
319	T	Phosphorylation	Kinase	MK14	Q16539	PhosphoELM
355	S	Phosphorylation	Kinase	MK07	Q13164	PhosphoELM
355	S	Phosphorylation	Kinase	P38-SUBFAMILY	-	GPS
408	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
408	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
453	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
453	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
453	S	Phosphorylation	Kinase	P38-SUBFAMILY	-	GPS
453	S	Phosphorylation	Kinase	MAPK	-	Uniprot
479	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
479	S	Phosphorylation	Kinase	P38-SUBFAMILY	-	GPS
494	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
4	K	Acetylation	16563226
Acetylation on Lys-4 increases DNA binding and transactivation (By similarity).
312	T	Phosphorylation	9858528
Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF.
312	T	Phosphorylation	9858528
Phosphorylation on Thr-312 and Thr-319 are the main sites involved in p38 MAPK signaling and activate transcription.
319	T	Phosphorylation	9858528
Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF.
319	T	Phosphorylation	9858528
Phosphorylation on Thr-312 and Thr-319 are the main sites involved in p38 MAPK signaling and activate transcription.
355	S	Phosphorylation	9858528
Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF.
403	K	Acetylation	16563226
Acetylation on Lys-403 activates transcriptional activity.
403	K	Sumoylation	16563226
Sumoylation on Lys-403 is enhanced by PIAS1 and represses transcriptional activity.
403	K	Sumoylation	16563226
Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation.
403	K	Sumoylation	16563226
Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site.
403	K	Phosphorylation	16563226
Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation.
403	K	Phosphorylation	16563226
Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site.
403	K	Acetylation	16563226
Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation.
403	K	Acetylation	16563226
Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site.
408	S	Acetylation	12586839
Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site.
408	S	Acetylation	12586839
Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation.
408	S	Phosphorylation	12586839
Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site.
408	S	Phosphorylation	12586839
Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation.
408	S	Phosphorylation	12586839
Phosphorylation on Ser-408 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons.
408	S	Phosphorylation	12586839
Phosphorylation on Ser-408 is required for sumoylation.
408	S	Sumoylation	12586839
Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site.
408	S	Sumoylation	12586839
Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation.
408	S	Sumoylation	12586839
Phosphorylation on Ser-408 is required for sumoylation.

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 MEF2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THA_HUMAN	THRA	physical	12371907
EP300_HUMAN	EP300	physical	12371907
HDAC5_HUMAN	HDAC5	physical	10748098
HDAC4_HUMAN	HDAC4	physical	10748098
HDAC9_HUMAN	HDAC9	physical	10748098
SMAD2_HUMAN	SMAD2	physical	11160896
ASCL1_HUMAN	ASCL1	physical	8662987
MEF2D_HUMAN	MEF2D	physical	8798771
ACTN4_HUMAN	ACTN4	physical	16980305
HDAC7_HUMAN	HDAC7	physical	16980305
HDAC4_HUMAN	HDAC4	physical	19389706
HDAC5_HUMAN	HDAC5	physical	12626519
HDAC7_HUMAN	HDAC7	physical	20590529
HDAC1_HUMAN	HDAC1	physical	20590529
NDUB9_HUMAN	NDUFB9	physical	21988832
GBB2_HUMAN	GNB2	physical	23326349
HDAC3_HUMAN	HDAC3	physical	22308472
HDAC5_HUMAN	HDAC5	physical	22308472
HDAC7_HUMAN	HDAC7	physical	22308472
HAND1_HUMAN	HAND1	physical	16043483
JUN_HUMAN	JUN	physical	25609649
ATF3_HUMAN	ATF3	physical	25609649
ATF7_HUMAN	ATF7	physical	25609649
CABIN_HUMAN	CABIN1	physical	25609649
H2B1A_HUMAN	HIST1H2BA	physical	25609649
MEF2C_HUMAN	MEF2C	physical	25609649
HIRA_HUMAN	HIRA	physical	25609649
MEF2D_HUMAN	MEF2D	physical	25609649
REV3L_HUMAN	REV3L	physical	25609649
SH2B1_HUMAN	SH2B1	physical	25609649
H31T_HUMAN	HIST3H3	physical	25609649
JUND_HUMAN	JUND	physical	25609649
CCD15_HUMAN	CCDC15	physical	25609649
MAPK3_HUMAN	MAPKAPK3	physical	25609649
SETX_HUMAN	SETX	physical	25609649
TTLL7_HUMAN	TTLL7	physical	25609649
ZCPW1_HUMAN	ZCWPW1	physical	25609649
HDAC5_HUMAN	HDAC5	physical	25609649
ITB1_HUMAN	ITGB1	physical	25609649
XYLT1_HUMAN	XYLT1	physical	25609649
TSR3_HUMAN	TSR3	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608320	Coronary artery disease, autosomal dominant, 1 (ADCAD1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MEF2A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-249, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-235, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-235 AND SER-255, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"A calcium-regulated MEF2 sumoylation switch controls postsynapticdifferentiation."; Shalizi A., Gaudilliere B., Yuan Z., Stegmueller J., Shirogane T.,Ge Q., Tan Y., Schulman B., Harper J.W., Bonni A.; Science 311:1012-1017(2006). Cited for: PHOSPHORYLATION AT SER-408, AND FUNCTION.	16484498 [Abstract]
"PDSM, a motif for phosphorylation-dependent SUMO modification."; Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,Nakai A., Sistonen L.; Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006). Cited for: SUMOYLATION AT LYS-403, PHOSPHORYLATION AT SER-408, FUNCTION, ANDMUTAGENESIS OF LYS-403 AND SER-408.	16371476 [Abstract]
"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-408, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-408.	12691662 [Abstract]
"Phosphorylation motifs regulating the stability and function ofmyocyte enhancer factor 2A."; Cox D.M., Du M., Marback M., Yang E.C.C., Chan J., Siu K.W.M.,McDermott J.C.; J. Biol. Chem. 278:15297-15303(2003). Cited for: PHOSPHORYLATION AT SER-255; THR-312; THR-319 AND SER-408, MASSSPECTROMETRY, AND MUTAGENESIS OF SER-255.	12586839 [Abstract]
"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 THR-312; THR-319 AND SER-355, AND MUTAGENESIS OFTHR-312; THR-319 AND SER-355.	10849446 [Abstract]
"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). Cited for: PHOSPHORYLATION AT THR-312; THR-319 AND SER-453, FUNCTION,HETERODIMERIZATION, AND MUTAGENESIS OF THR-312; THR-319; SER-355;SER-453 AND SER-479.	9858528 [Abstract]
"Nemo-like kinase-myocyte enhancer factor 2A signaling regulatesanterior formation in Xenopus development."; Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T.,Shibuya H.; Mol. Cell. Biol. 27:7623-7630(2007). Cited for: PHOSPHORYLATION AT THR-312 BY NLK.	17785444 [Abstract]
"Targeting of p38 mitogen-activated protein kinases to MEF2transcription factors."; Yang S.-H., Galanis A., Sharrocks A.D.; Mol. Cell. Biol. 19:4028-4038(1999). Cited for: INTERACTION WITH MAPK14, PHOSPHORYLATION AT THR-312 AND THR-319, ANDMUTAGENESIS OF ARG-269; LYS-270; LEU-273; VAL-275; ILE-277 ANDPRO-278.	10330143 [Abstract]
Sumoylation
Reference	PubMed
"PDSM, a motif for phosphorylation-dependent SUMO modification."; Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,Nakai A., Sistonen L.; Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006). Cited for: SUMOYLATION AT LYS-403, PHOSPHORYLATION AT SER-408, FUNCTION, ANDMUTAGENESIS OF LYS-403 AND SER-408.	16371476 [Abstract]
"SUMO-1 modification of MEF2A regulates its transcriptionalactivity."; Riquelme C., Barthel K.K., Liu X.; J. Cell. Mol. Med. 10:132-144(2006). Cited for: SUMOYLATION AT LYS-403, INTERACTION WITH PIAS1, FUNCTION, SUBCELLULARLOCATION, AND MUTAGENESIS OF LYS-403.	16563226 [Abstract]

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