dbPTM

HDAC4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HDAC4_HUMAN
UniProt AC	P56524
Protein Name	Histone deacetylase 4
Gene Name	HDAC4
Organism	Homo sapiens (Human).
Sequence Length	1084
Subcellular Localization	Nucleus. Cytoplasm. Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on
Protein Description	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1. [PubMed: 27708256]
Protein Sequence	MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSQSHPDG ------CCCCCCCCC	48.68	25599653
3	Phosphorylation	-----MSSQSHPDGL -----CCCCCCCCCC	47.78	27251275
5	Phosphorylation	---MSSQSHPDGLSG ---CCCCCCCCCCCC	38.65	27251275
11	Phosphorylation	QSHPDGLSGRDQPVE CCCCCCCCCCCCCCH	36.99	20068231
36	Phosphorylation	PSTVDVATALPLQVA CCCCCHHHHCCCEEC	28.68	27251275
45	Phosphorylation	LPLQVAPSAVPMDLR CCCEECCCCCCCCEE	31.96	27251275
58	Phosphorylation	LRLDHQFSLPVAEPA EECCCCCCCCCCCHH	25.78	28857561
79	Ubiquitination	QQELLALKQKQQIQR HHHHHHHHHHHHHHH	50.25	29967540
151	Ubiquitination	EKQHREQKLQQLKNK HHHHHHHHHHHHHHH	43.44	29967540
168	Phosphorylation	GKESAVASTEVKMKL CCHHHCCHHHHHHHH	20.64	-
196	Phosphorylation	RNLNHCISSDPRYWY CCCCHHHCCCCCCCC	33.80	28450419
197	Phosphorylation	NLNHCISSDPRYWYG CCCHHHCCCCCCCCC	31.55	28450419
206	Phosphorylation	PRYWYGKTQHSSLDQ CCCCCCCCCCCCCCC	27.44	23401153
209	Phosphorylation	WYGKTQHSSLDQSSP CCCCCCCCCCCCCCC	23.84	28450419
210	Phosphorylation	YGKTQHSSLDQSSPP CCCCCCCCCCCCCCC	33.56	25159151
214	Phosphorylation	QHSSLDQSSPPQSGV CCCCCCCCCCCCCCC	44.47	28450419
215	Phosphorylation	HSSLDQSSPPQSGVS CCCCCCCCCCCCCCC	34.66	26657352
219	Phosphorylation	DQSSPPQSGVSTSYN CCCCCCCCCCCCCCC	47.11	28450419
222	Phosphorylation	SPPQSGVSTSYNHPV CCCCCCCCCCCCCCC	18.37	30576142
223	Phosphorylation	PPQSGVSTSYNHPVL CCCCCCCCCCCCCCC	32.59	30576142
224	Phosphorylation	PQSGVSTSYNHPVLG CCCCCCCCCCCCCCC	19.21	28450419
225	Phosphorylation	QSGVSTSYNHPVLGM CCCCCCCCCCCCCCC	19.99	28450419
233	Phosphorylation	NHPVLGMYDAKDDFP CCCCCCCEECCCCCC	15.79	26074081
236	Acetylation	VLGMYDAKDDFPLRK CCCCEECCCCCCCCC	55.74	20167786
243	Ubiquitination	KDDFPLRKTASEPNL CCCCCCCCCCCCCCH	57.01	-
244	Phosphorylation	DDFPLRKTASEPNLK CCCCCCCCCCCCCHH	29.05	30183078
246	Phosphorylation	FPLRKTASEPNLKLR CCCCCCCCCCCHHHH	59.84	25159151
251	Acetylation	TASEPNLKLRSRLKQ CCCCCCHHHHHHHHH	48.79	25953088
265	Phosphorylation	QKVAERRSSPLLRRK HHHHHHHCCCCHHCC	42.39	25159151
266	Phosphorylation	KVAERRSSPLLRRKD HHHHHHCCCCHHCCC	20.11	26846344
278	Phosphorylation	RKDGPVVTALKKRPL CCCCCCEEEEECCCC	26.89	18491316
281	Acetylation	GPVVTALKKRPLDVT CCCEEEEECCCCCCC	44.25	25953088
288	Phosphorylation	KKRPLDVTDSACSSA ECCCCCCCCCCCCCC	24.73	20873877
290	Phosphorylation	RPLDVTDSACSSAPG CCCCCCCCCCCCCCC	23.08	20873877
293	Phosphorylation	DVTDSACSSAPGSGP CCCCCCCCCCCCCCC	29.29	20873877
294	Phosphorylation	VTDSACSSAPGSGPS CCCCCCCCCCCCCCC	38.06	20873877
298	Phosphorylation	ACSSAPGSGPSSPNN CCCCCCCCCCCCCCC	46.61	20873877
301	Phosphorylation	SAPGSGPSSPNNSSG CCCCCCCCCCCCCCC	63.05	30576142
302	Phosphorylation	APGSGPSSPNNSSGS CCCCCCCCCCCCCCC	34.48	30576142
306	Phosphorylation	GPSSPNNSSGSVSAE CCCCCCCCCCCCCCC	42.59	20873877
307	Phosphorylation	PSSPNNSSGSVSAEN CCCCCCCCCCCCCCC	36.89	20873877
309	Phosphorylation	SPNNSSGSVSAENGI CCCCCCCCCCCCCCC	18.17	20873877
311	Phosphorylation	NNSSGSVSAENGIAP CCCCCCCCCCCCCCC	31.40	20873877
321	Ubiquitination	NGIAPAVPSIPAETS CCCCCCCCCCCCCCC	28.75	-
322	Phosphorylation	GIAPAVPSIPAETSL CCCCCCCCCCCCCCH	34.31	20873877
327	Phosphorylation	VPSIPAETSLAHRLV CCCCCCCCCHHHHHH	31.02	20873877
328	Phosphorylation	PSIPAETSLAHRLVA CCCCCCCCHHHHHHH	18.31	20873877
339	Phosphorylation	RLVAREGSAAPLPLY HHHHCCCCCCCCCCC	19.26	28464451
346	Phosphorylation	SAAPLPLYTSPSLPN CCCCCCCCCCCCCCC	11.84	27080861
347	Phosphorylation	AAPLPLYTSPSLPNI CCCCCCCCCCCCCCE	41.67	27080861
348	Phosphorylation	APLPLYTSPSLPNIT CCCCCCCCCCCCCEE	10.03	29802988
350	Phosphorylation	LPLYTSPSLPNITLG CCCCCCCCCCCEEEE	57.11	28857561
355	Phosphorylation	SPSLPNITLGLPATG CCCCCCEEEECCCCC	22.78	27080861
361	Phosphorylation	ITLGLPATGPSAGTA EEEECCCCCCCCCCC	47.92	27080861
364	Phosphorylation	GLPATGPSAGTAGQQ ECCCCCCCCCCCCHH	40.45	27080861
367	Phosphorylation	ATGPSAGTAGQQDAE CCCCCCCCCCHHHHH	27.60	27080861
391	Phosphorylation	RLSLFPGTHLTPYLS HHCCCCCCCCCCCCC	17.60	21712546
394	Phosphorylation	LFPGTHLTPYLSTSP CCCCCCCCCCCCCCC	11.41	21712546
396	Phosphorylation	PGTHLTPYLSTSPLE CCCCCCCCCCCCCCC	14.19	28450419
398	Phosphorylation	THLTPYLSTSPLERD CCCCCCCCCCCCCCC	22.46	28450419
399	Phosphorylation	HLTPYLSTSPLERDG CCCCCCCCCCCCCCC	31.59	28450419
400	Phosphorylation	LTPYLSTSPLERDGG CCCCCCCCCCCCCCC	24.90	28450419
465	Phosphorylation	QHRPLGRTQSAPLPQ HCCCCCCCCCCCCCC	25.69	23927012
467	Phosphorylation	RPLGRTQSAPLPQNA CCCCCCCCCCCCCHH	31.10	23927012
472	Phosphorylation	TQSAPLPQNAQALQH CCCCCCCCHHHHHHH	66.62	32142685
494	Ubiquitination	QQFLEKHKQQFQQQQ HHHHHHHHHHHHHHH	57.79	29967540
540	Phosphorylation	QALLDEPYLDRLPGQ HHHHCCHHHHCCCCC	21.13	27642862
548	Acetylation	LDRLPGQKEAHAQAG HHCCCCCHHHHHHHC	63.88	7834049
559	Sumoylation	AQAGVQVKQEPIESD HHHCCCCCCCCCCCC	31.67	12032081
559	Sumoylation	AQAGVQVKQEPIESD HHHCCCCCCCCCCCC	31.67	-
565	Phosphorylation	VKQEPIESDEEEAEP CCCCCCCCCCCCCCC	51.55	29255136
570	Phosphorylation	IESDEEEAEPPREVE CCCCCCCCCCCCCCC	37.56	33259812
584	Phosphorylation	EPGQRQPSEQELLFR CCCCCCCCHHHHHHH	43.50	26074081
610	Ubiquitination	HQLRNYQASMEAAGI HHHHHHHHHHHHHCC	10.65	-
611	Phosphorylation	QLRNYQASMEAAGIP HHHHHHHHHHHHCCC	11.13	26437602
620	Phosphorylation	EAAGIPVSFGGHRPL HHHCCCCCCCCCCCC	16.90	28348404
628	Phosphorylation	FGGHRPLSRAQSSPA CCCCCCCCCCCCCCC	28.40	28348404
632	Phosphorylation	RPLSRAQSSPASATF CCCCCCCCCCCCCCC	36.99	29255136
633	Phosphorylation	PLSRAQSSPASATFP CCCCCCCCCCCCCCC	16.65	29255136
636	Phosphorylation	RAQSSPASATFPVSV CCCCCCCCCCCCCCC	31.09	23927012
637	Phosphorylation	AQSSPASATFPVSVQ CCCCCCCCCCCCCCC	18.50	32645325
638	Phosphorylation	QSSPASATFPVSVQE CCCCCCCCCCCCCCC	26.44	23927012
642	Phosphorylation	ASATFPVSVQEPPTK CCCCCCCCCCCCCCC	20.51	23927012
642	O-linked_Glycosylation	ASATFPVSVQEPPTK CCCCCCCCCCCCCCC	20.51	31195810
643	Phosphorylation	SATFPVSVQEPPTKP CCCCCCCCCCCCCCC	8.33	32142685
648	Phosphorylation	VSVQEPPTKPRFTTG CCCCCCCCCCCCCCC	65.48	23927012
658	Phosphorylation	RFTTGLVYDTLMLKH CCCCCHHHHHHHHEE	14.30	29116813
684	Phosphorylation	EHAGRIQSIWSRLQE HHHHHHHHHHHHHHH	24.53	28857561
705	Ubiquitination	CECIRGRKATLEELQ CEECCCCCCCHHHHH	48.85	29967540
737	Ubiquitination	RQKLDSKKLLGSLAS HHHCCHHHHHHHHHH	53.55	-
741	Phosphorylation	DSKKLLGSLASVFVR CHHHHHHHHHHHHHC	22.26	-
744	Phosphorylation	KLLGSLASVFVRLPC HHHHHHHHHHHCCCC	22.75	-
830	Phosphorylation	KLLQQRLSVSKILIV HHHHHHHCCCEEEEE	26.91	24719451
1025	Phosphorylation	EKVMEIHSKYWRCLQ HHHHHHHHHHHHHHH	32.85	-
1026	Ubiquitination	KVMEIHSKYWRCLQR HHHHHHHHHHHHHHH	34.37	29967540
1034	Phosphorylation	YWRCLQRTTSTAGRS HHHHHHHHCCHHCCC	16.49	20068231
1036	Phosphorylation	RCLQRTTSTAGRSLI HHHHHHCCHHCCCHH	18.69	26546556
1057	Phosphorylation	NEEAETVTAMASLSV CCCHHHHHHHHHHCC	20.38	-
1061	Phosphorylation	ETVTAMASLSVGVKP HHHHHHHHHCCCCCC	14.21	-
1078	Sulfoxidation	KRPDEEPMEEEPPL- HCCCCCCCCCCCCC-	13.16	21406390

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
210	S	Phosphorylation	Kinase	CAMK2D	Q13557	PSP
246	S	Phosphorylation	Kinase	SIK1	P57059	Uniprot
246	S	Phosphorylation	Kinase	MARK2	Q7KZI7	PSP
246	S	Phosphorylation	Kinase	CAMK4	Q16566	Uniprot
246	S	Phosphorylation	Kinase	MAP3K7	O43318	GPS
265	S	Phosphorylation	Kinase	PKACA	P17612	PSP
265	S	Phosphorylation	Kinase	PKACA	P05132	PSP
266	S	Phosphorylation	Kinase	PKACA	P17612	PSP
266	S	Phosphorylation	Kinase	PKACA	P05132	PSP
298	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
302	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
467	S	Phosphorylation	Kinase	KKCC1	Q8N5S9	PhosphoELM
467	S	Phosphorylation	Kinase	CAMK4	Q16566	Uniprot
467	S	Phosphorylation	Kinase	SIK1	P57059	Uniprot
584	S	Phosphorylation	Kinase	PKACA	P17612	PSP
632	S	Phosphorylation	Kinase	CAMK4	Q16566	Uniprot
632	S	Phosphorylation	Kinase	KKCC1	Q8N5S9	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
246	S	Phosphorylation	10958686
Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632.
350	S	Phosphorylation	19690332
Phosphorylation at Ser-350, within the PxLPxI/L motif, impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3.
467	S	Phosphorylation	10958686
Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632.
559	K	Phosphorylation	12032081
Sumoylation on Lys-559 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.
559	K	Sumoylation	12032081
Sumoylation on Lys-559 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.
632	S	Phosphorylation	10958686
Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632.

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 HDAC4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBT16_HUMAN	ZBTB16	physical	15467736
CTBP1_HUMAN	CTBP1	physical	11022042
CTBP1_MOUSE	Ctbp1	physical	11022042
GATA1_HUMAN	GATA1	physical	14668799
MEF2A_HUMAN	MEF2A	physical	10487761
MEF2C_HUMAN	MEF2C	physical	10523670
MEF2D_HUMAN	MEF2D	physical	10523670
HDAC4_HUMAN	HDAC4	physical	11486037
NR2C1_HUMAN	NR2C1	physical	11463856
RBBP4_HUMAN	RBBP4	physical	10220385
HDAC3_HUMAN	HDAC3	physical	10220385
HDAC3_HUMAN	HDAC3	physical	11804585
NCOR1_HUMAN	NCOR1	physical	11804585
NCOR2_HUMAN	NCOR2	physical	11804585
HDAC3_HUMAN	HDAC3	physical	11466315
BCL6_HUMAN	BCL6	physical	11929873
ZBT16_HUMAN	ZBTB16	physical	11929873
NCOR1_HUMAN	NCOR1	physical	10640275
NCOR2_HUMAN	NCOR2	physical	10640275
1433B_HUMAN	YWHAB	physical	10869435
1433E_HUMAN	YWHAE	physical	10869435
HDAC3_HUMAN	HDAC3	physical	10869435
EVI1_HUMAN	MECOM	physical	11568182
SUV91_HUMAN	SUV39H1	physical	12242305
NCOR2_MOUSE	Ncor2	physical	11509652
MK03_HUMAN	MAPK3	physical	11114188
MK01_HUMAN	MAPK1	physical	11114188
FOXP3_HUMAN	FOXP3	physical	19276356
DNJB8_HUMAN	DNAJB8	physical	20159555
DNJB6_HUMAN	DNAJB6	physical	20159555
ATF2_HUMAN	ATF2	physical	20116378
RUNX2_HUMAN	RUNX2	physical	20097749
SENP1_HUMAN	SENP1	physical	20079608
CDK5_HUMAN	CDK5	physical	16356933
PRKN_HUMAN	PARK2	physical	16332688
NR1H2_HUMAN	NR1H2	physical	17218271
HIF1A_HUMAN	HIF1A	physical	19071119
KCC2D_HUMAN	CAMK2D	physical	17179159
TYY1_HUMAN	YY1	physical	19013255
CREST_HUMAN	SS18L1	physical	20211142
SP1_HUMAN	SP1	physical	18850004
REST_HUMAN	REST	physical	17011572
SIN3A_HUMAN	SIN3A	physical	17011572
MARK3_HUMAN	MARK3	physical	16980613
HIF1A_HUMAN	HIF1A	physical	16951198
KCC2D_HUMAN	CAMK2D	physical	16767219
KCC1A_HUMAN	CAMK1	physical	16767219
GCM1_HUMAN	GCM1	physical	16528103
MEF2D_HUMAN	MEF2D	physical	16356933
NU214_HUMAN	NUP214	physical	16356933
TYY1_HUMAN	YY1	physical	18558095
DNJB5_HUMAN	DNAJB5	physical	18555775
ESCO2_HUMAN	ESCO2	physical	18501190
GBB1_HUMAN	GNB1	physical	16221676
TP53B_HUMAN	TP53BP1	physical	12668657
SRF_HUMAN	SRF	physical	12663674
UBC9_HUMAN	UBE2I	physical	16166628
HNF4A_HUMAN	HNF4A	physical	12205093
ESR1_HUMAN	ESR1	physical	16051668
MEF2C_HUMAN	MEF2C	physical	15964851
1433T_HUMAN	YWHAQ	physical	15964851
ANRA2_HUMAN	ANKRA2	physical	15964851
ATRX_HUMAN	ATRX	physical	15964851
REV3L_HUMAN	REV3L	physical	15964851
MAP1S_HUMAN	MAP1S	physical	15964851
RFXK_HUMAN	RFXANK	physical	15964851
C2TA_HUMAN	CIITA	physical	15964851
PP2AA_HUMAN	PPP2CA	physical	18339811
IKBA_HUMAN	NFKBIA	physical	15536134
HDAC4_HUMAN	HDAC4	physical	18332106
HDAC5_HUMAN	HDAC5	physical	18332106
MEF2C_HUMAN	MEF2C	physical	18332106
1433T_HUMAN	YWHAQ	physical	11470791
CSRP3_HUMAN	CSRP3	physical	18250163
1433B_HUMAN	YWHAB	physical	10958686
NU155_HUMAN	NUP155	physical	21464227
ATX1_HUMAN	ATXN1	physical	17646162
ANDR_HUMAN	AR	physical	21242980
TWST1_MOUSE	Twist1	physical	19950203
NFKB1_HUMAN	NFKB1	physical	12917325
SF01_HUMAN	SF1	physical	12917325
KDM5B_HUMAN	KDM5B	physical	17373667
1433T_HUMAN	YWHAQ	physical	22466704
2AAA_HUMAN	PPP2R1A	physical	22466704
PP2AA_HUMAN	PPP2CA	physical	22466704
STAT1_HUMAN	STAT1	physical	21571862
NFAC1_HUMAN	NFATC1	physical	19218564
HIF1A_HUMAN	HIF1A	physical	21148070
NACC1_HUMAN	NACC1	physical	16033423
ZBT16_HUMAN	ZBTB16	physical	19648967
JDP2_HUMAN	JDP2	physical	22989952
ATF3_HUMAN	ATF3	physical	22989952
A4_HUMAN	APP	physical	21832049
ZBT7B_HUMAN	ZBTB7B	physical	22730529
HDAC5_HUMAN	HDAC5	physical	22730529
1433T_HUMAN	YWHAQ	physical	17470459
1433B_HUMAN	YWHAB	physical	23752268
1433E_HUMAN	YWHAE	physical	23752268
1433F_HUMAN	YWHAH	physical	23752268
1433G_HUMAN	YWHAG	physical	23752268
1433S_HUMAN	SFN	physical	23752268
1433T_HUMAN	YWHAQ	physical	23752268
1433Z_HUMAN	YWHAZ	physical	23752268
TBL1R_HUMAN	TBL1XR1	physical	23752268
HDAC4_HUMAN	HDAC4	physical	23752268
NCOR1_HUMAN	NCOR1	physical	23752268
SIR1_HUMAN	SIRT1	physical	23417673
MI4GD_HUMAN	MIF4GD	physical	21988832
1433T_HUMAN	YWHAQ	physical	23393134
MTUS2_HUMAN	MTUS2	physical	25416956
LDOC1_HUMAN	LDOC1	physical	25416956
FBLN4_HUMAN	EFEMP2	physical	25416956
ANRA2_HUMAN	ANKRA2	physical	25416956
RINT1_HUMAN	RINT1	physical	25416956
CC136_HUMAN	CCDC136	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
MEF2D_HUMAN	MEF2D	physical	16166628
CBX5_MOUSE	Cbx5	physical	12242305
ANRA2_HUMAN	ANKRA2	physical	25752541
CUL7_HUMAN	CUL7	physical	25752541
PPARG_HUMAN	PPARG	physical	21605119
CING_HUMAN	CGN	physical	27173435
MAGI1_HUMAN	MAGI1	physical	27173435
SYDE1_HUMAN	SYDE1	physical	27173435
F110B_HUMAN	FAM110B	physical	27173435
F110A_HUMAN	FAM110A	physical	27173435
KIF1C_HUMAN	KIF1C	physical	27173435
NAV1_HUMAN	NAV1	physical	27173435
BTG2_RAT	Btg2	physical	27333946
BTG2_RAT	Btg2	physical	17371797

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600430	Brachydactyly-mental retardation syndrome (BDMR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HDAC4_HUMAN

Related Literatures of Post-Translational Modification

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-350, 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-565; SER-632 ANDSER-633, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Regulation of histone deacetylase 4 by binding of 14-3-3 proteins."; Wang A.H., Kruhlak M.J., Wu J., Bertos N.R., Vezmar M., Posner B.I.,Bazett-Jones D.P., Yang X.-J.; Mol. Cell. Biol. 20:6904-6912(2000). Cited for: PHOSPHORYLATION AT SER-246; SER-467 AND SER-632, AND MUTAGENESIS OFSER-246; SER-467 AND SER-632.	10958686 [Abstract]
Sumoylation
Reference	PubMed
"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4deacetylase."; Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.; EMBO J. 21:2682-2691(2002). Cited for: HOMODIMERIZATION, SUMOYLATION AT LYS-559, AND MUTAGENESIS OF LYS-559.	12032081 [Abstract]

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