dbPTM

SMAD4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMAD4_HUMAN
UniProt AC	Q13485
Protein Name	Mothers against decapentaplegic homolog 4
Gene Name	SMAD4
Organism	Homo sapiens (Human).
Sequence Length	552
Subcellular Localization	Cytoplasm . Nucleus . Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with R-SMAD (PubMed:15799969). PDPK1 prevents its nuclear translocation in response to TGF-beta (PubMed:17327236).
Protein Description	In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator..
Protein Sequence	MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSSMMVKDEYVHDFEGQPSLSTEGHSIQTIQHPPSNRASTETYSTPALLAPSESNATSTANFPNIPVASTSQPASILGGSHSEGLLQIASGPQPGQQQNGFTGQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MDNMSITNTPTSND -CCCCCCCCCCCCHH	26.23	24719451
9	Phosphorylation	DNMSITNTPTSNDAC CCCCCCCCCCCHHHH	21.20	25159151
22	Phosphorylation	ACLSIVHSLMCHRQG HHHHHHHHHHHHCCC	13.60	-
32	Phosphorylation	CHRQGGESETFAKRA HHCCCCCCHHHHHHH	45.25	-
37	Acetylation	GESETFAKRAIESLV CCCHHHHHHHHHHHH	37.87	19608861
42	Phosphorylation	FAKRAIESLVKKLKE HHHHHHHHHHHHHHH	32.14	26546556
45	Ubiquitination	RAIESLVKKLKEKKD HHHHHHHHHHHHCHH	58.65	19608861
45	Malonylation	RAIESLVKKLKEKKD HHHHHHHHHHHHCHH	58.65	26320211
45	Acetylation	RAIESLVKKLKEKKD HHHHHHHHHHHHCHH	58.65	23749302
48	Acetylation	ESLVKKLKEKKDELD HHHHHHHHHCHHHHH	76.11	155683
59	O-linked_Glycosylation	DELDSLITAITTNGA HHHHHHHHHHHCCCC	19.80	33199824
62	O-linked_Glycosylation	DSLITAITTNGAHPS HHHHHHHHCCCCCHH	16.25	33199824
63	O-linked_Glycosylation	SLITAITTNGAHPSK HHHHHHHCCCCCHHH	26.07	33199824
69	O-linked_Glycosylation	TTNGAHPSKCVTIQR HCCCCCHHHCEEEEE	28.90	33199824
70	Ubiquitination	TNGAHPSKCVTIQRT CCCCCHHHCEEEEEE	36.86	-
77	Phosphorylation	KCVTIQRTLDGRLQV HCEEEEEECCCCEEE	16.90	20974850
88	Malonylation	RLQVAGRKGFPHVIY CEEECCCCCCCHHHH	65.08	26320211
95	Phosphorylation	KGFPHVIYARLWRWP CCCCHHHHEECCCCC	5.65	27642862
106	Acetylation	WRWPDLHKNELKHVK CCCCCCCHHHCCCCC	60.46	19608861
113	Sumoylation	KNELKHVKYCQYAFD HHHCCCCCCCCCCCC	39.77	-
113	Ubiquitination	KNELKHVKYCQYAFD HHHCCCCCCCCCCCC	39.77	21890473
113	Sumoylation	KNELKHVKYCQYAFD HHHCCCCCCCCCCCC	39.77	28112733
122	Ubiquitination	CQYAFDLKCDSVCVN CCCCCCCCCCEEEEC	37.53	-
138	Phosphorylation	YHYERVVSPGIDLSG HHHEEECCCCCCCCC	17.98	27050516
144	Phosphorylation	VSPGIDLSGLTLQSN CCCCCCCCCCEECCC	28.19	29523821
147	Phosphorylation	GIDLSGLTLQSNAPS CCCCCCCEECCCCCC	26.69	28555341
155	Phosphorylation	LQSNAPSSMMVKDEY ECCCCCCCCEECCCE	15.16	28555341
159	Sumoylation	APSSMMVKDEYVHDF CCCCCEECCCEEECC	27.26	-
159	Sumoylation	APSSMMVKDEYVHDF CCCCCEECCCEEECC	27.26	-
162	Phosphorylation	SMMVKDEYVHDFEGQ CCEECCCEEECCCCC	17.14	28796482
171	Phosphorylation	HDFEGQPSLSTEGHS ECCCCCCCCCCCCCC	27.37	28555341
178	Phosphorylation	SLSTEGHSIQTIQHP CCCCCCCCEEEEECC	27.52	28555341
206	O-linked_Glycosylation	ALLAPSESNATSTAN CCCCCCCCCCCCCCC	35.78	33199824
209	O-linked_Glycosylation	APSESNATSTANFPN CCCCCCCCCCCCCCC	30.75	33199824
211	O-linked_Glycosylation	SESNATSTANFPNIP CCCCCCCCCCCCCCC	22.67	33199824
221	O-linked_Glycosylation	FPNIPVASTSQPASI CCCCCCCCCCCCCHH	28.91	33199824
223	O-linked_Glycosylation	NIPVASTSQPASILG CCCCCCCCCCCHHHC	31.50	33199824
265	Phosphorylation	ATYHHNSTTTWTGSR CEECCCCCCEEECCC	33.30	-
269	Phosphorylation	HNSTTTWTGSRTAPY CCCCCEEECCCCCCC	24.16	-
273	Phosphorylation	TTWTGSRTAPYTPNL CEEECCCCCCCCCCC	33.41	-
277	Phosphorylation	GSRTAPYTPNLPHHQ CCCCCCCCCCCCCCC	12.49	12801888
343	Phosphorylation	GETFKVPSSCPIVTV CCEEECCCCCCEEEE	47.78	22817900
385	Ubiquitination	RARLHIGKGVQLECK HHHCCCCCCCEEEEC	56.13	-
428	Acetylation	APGDAVHKIYPSAYI CCCCHHHHHCCHHEE	37.02	19608861
428	Malonylation	APGDAVHKIYPSAYI CCCCHHHHHCCHHEE	37.02	26320211
430	Phosphorylation	GDAVHKIYPSAYIKV CCHHHHHCCHHEEEE	8.92	28152594
432	Phosphorylation	AVHKIYPSAYIKVFD HHHHHCCHHEEEEEE	19.41	28152594
434	Phosphorylation	HKIYPSAYIKVFDLR HHHCCHHEEEEEEHH	12.95	28152594
504	Phosphorylation	RLCILRMSFVKGWGP HHHHHHHHHHCCCCC	22.06	24719451
507	Ubiquitination	ILRMSFVKGWGPDYP HHHHHHHCCCCCCCC	47.11	19608861
507	Acetylation	ILRMSFVKGWGPDYP HHHHHHHCCCCCCCC	47.11	19608861
507	Malonylation	ILRMSFVKGWGPDYP HHHHHHHCCCCCCCC	47.11	26320211
513	Phosphorylation	VKGWGPDYPRQSIKE HCCCCCCCCCCCCCC	11.93	24719451
519	Ubiquitination	DYPRQSIKETPCWIE CCCCCCCCCCCCEEE	61.86	21890473
543	Sulfoxidation	LDEVLHTMPIADPQP HHHHHHHCCCCCCCC	1.25	30846556

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
9	T	Phosphorylation	Kinase	NLK	Q9UBE8	PSP
77	T	Phosphorylation	Kinase	STK11	Q15831	GPS
138	S	Phosphorylation	Kinase	NLK	Q9UBE8	PSP
265	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
269	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
273	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
277	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
343	S	Phosphorylation	Kinase	MELK	Q61846	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM33	Q9UPN9	PMID:15820681
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF2	Q9HAU4	PMID:15817471
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:14988407
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:15314162
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:14701756
-	K	Ubiquitination	E3 ubiquitin ligase	WWP1	Q9H0M0	PMID:15817471

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
519	K	ubiquitylation		19135894
Monoubiquitinated on Lys-519 by E3 ubiquitin-protein ligase TRIM33.

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 SMAD4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHOG_MOUSE	Rhog	physical	15761153
RHES_MOUSE	Rasd2	physical	15761153
RAB13_MOUSE	Rab13	physical	15761153
RHOJ_MOUSE	Rhoj	physical	15761153
RAB2B_MOUSE	Rab2b	physical	15761153
RHOD_MOUSE	Rhod	physical	15761153
RAC2_MOUSE	Rac2	physical	15761153
RAB3B_MOUSE	Rab3b	physical	15761153
RAB38_MOUSE	Rab38	physical	15761153
RRAS2_MOUSE	Rras2	physical	15761153
ARFRP_MOUSE	Arfrp1	physical	15761153
ARL5B_MOUSE	Arl5b	physical	15761153
ARHG7_MOUSE	Arhgef7	physical	15761153
SQSTM_MOUSE	Sqstm1	physical	15761153
NEK6_MOUSE	Nek6	physical	15761153
STK35_MOUSE	Stk35	physical	15761153
RIPK2_MOUSE	Ripk2	physical	15761153
MP2K3_MOUSE	Map2k3	physical	15761153
CHK1_MOUSE	Chek1	physical	15761153
E2AK4_MOUSE	Eif2ak4	physical	15761153
NUAK2_MOUSE	Nuak2	physical	15761153
TSSK3_MOUSE	Tssk3	physical	15761153
TOPK_MOUSE	Pbk	physical	15761153
UHMK1_MOUSE	Uhmk1	physical	15761153
PLK4_MOUSE	Plk4	physical	15761153
ILKAP_MOUSE	Ilkap	physical	15761153
TRI35_MOUSE	Trim35	physical	15761153
RNF14_MOUSE	Rnf14	physical	15761153
RN138_MOUSE	Rnf138	physical	15761153
SMAD1_MOUSE	Smad1	physical	15761153
SMAD3_MOUSE	Smad3	physical	15761153
OCLN_MOUSE	Ocln	physical	15761153
HDGF_MOUSE	Hdgf	physical	15761153
RAB34_MOUSE	Rab34	physical	15761153
UBB_MOUSE	Ubb	physical	15761153
RS27A_MOUSE	Rps27a	physical	15761153
ITK_MOUSE	Itk	physical	15761153
AP2B1_MOUSE	Ap2b1	physical	15761153
SMAD2_MOUSE	Smad2	physical	15761153
APBB2_MOUSE	Apbb2	physical	15761153
SMAD9_HUMAN	SMAD9	physical	16189514
UBC9_HUMAN	UBE2I	physical	16189514
FOXO3_HUMAN	FOXO3	physical	15084259
FOXO1_HUMAN	FOXO1	physical	15084259
FOXO4_HUMAN	FOXO4	physical	15084259
FBW1A_HUMAN	BTRC	physical	14988407
PIAS3_HUMAN	PIAS3	physical	14691252
DLX1_HUMAN	DLX1	physical	14671321
EID2_HUMAN	EID2	physical	14612439
SKI_HUMAN	SKI	physical	12874272
SMAD3_HUMAN	SMAD3	physical	12794086
SMAD2_HUMAN	SMAD2	physical	12794086
DVL1_HUMAN	DVL1	physical	12650946
ERBIN_HUMAN	ERBB2IP	physical	12650946
ATF2_HUMAN	ATF2	physical	10085140
RBL1_HUMAN	RBL1	physical	12150994
CTNB1_HUMAN	CTNNB1	physical	12000714
SKIL_HUMAN	SKIL	physical	10531062
SKI_HUMAN	SKI	physical	10531062
TFE3_HUMAN	TFE3	physical	12551947
MAX_HUMAN	MAX	physical	12551947
AKT1_HUMAN	AKT1	physical	16362038
SMAD2_HUMAN	SMAD2	physical	11027280
SMAD2_HUMAN	SMAD2	physical	9288972
DCP1A_HUMAN	DCP1A	physical	11836524
ANDR_HUMAN	AR	physical	12226080
JUNB_HUMAN	JUNB	physical	10220381
SMAD2_HUMAN	SMAD2	physical	10531362
SMAD5_HUMAN	SMAD5	physical	10531362
SMAD3_HUMAN	SMAD3	physical	10531362
SMAD1_HUMAN	SMAD1	physical	10531362
SNW1_HUMAN	SNW1	physical	11278756
SMAD7_HUMAN	SMAD7	genetic	9892009
CSN5_HUMAN	COPS5	physical	11818334
CEBPA_HUMAN	CEBPA	physical	12524424
CEBPB_HUMAN	CEBPB	physical	12524424
CEBPD_HUMAN	CEBPD	physical	12524424
TGFA1_HUMAN	TGFBRAP1	physical	11278302
SMAD6_HUMAN	SMAD6	physical	9256479
SMAD2_HUMAN	SMAD2	physical	18783722
FBW1A_HUMAN	BTRC	physical	16865698
SKP2_HUMAN	SKP2	physical	16865698
SMAD7_HUMAN	SMAD7	physical	15817471
SMAD2_HUMAN	SMAD2	physical	15817471
SMUF1_HUMAN	SMURF1	physical	15817471
FBW1A_HUMAN	BTRC	physical	15314162
PIAS4_HUMAN	PIAS4	physical	12904571
SMAD2_HUMAN	SMAD2	physical	12808092
TYY1_HUMAN	YY1	physical	12808092
SKI_HUMAN	SKI	physical	12732634
EVI1_HUMAN	MECOM	physical	15849193
SUMO1_HUMAN	SUMO1	physical	12740389
DAXX_HUMAN	DAXX	physical	15637079
UBC9_HUMAN	UBE2I	physical	15637079
SMAD7_HUMAN	SMAD7	physical	17438144
HDAC1_HUMAN	HDAC1	physical	14699069
SKI_HUMAN	SKI	physical	14699069
SMAD1_HUMAN	SMAD1	physical	21454478
SMAD2_HUMAN	SMAD2	physical	21454478
NKX25_HUMAN	NKX2-5	physical	21152044
SMAD3_HUMAN	SMAD3	physical	22045334
CHIP_HUMAN	STUB1	physical	14701756
USP9X_HUMAN	USP9X	physical	19135894
SMAD2_HUMAN	SMAD2	physical	19135894
SMAD3_HUMAN	SMAD3	physical	19135894
EP300_HUMAN	EP300	physical	9679056
SP1_HUMAN	SP1	physical	10878024
SMAD2_HUMAN	SMAD2	physical	10878024
SMAD3_HUMAN	SMAD3	physical	10878024
SMAD3_HUMAN	SMAD3	physical	10995777
HNF4A_HUMAN	HNF4A	physical	10995777
NU214_HUMAN	NUP214	physical	12917407
UBP15_HUMAN	USP15	physical	21947082
FOXO3_HUMAN	FOXO3	physical	21532621
SMAD2_HUMAN	SMAD2	physical	21532621
SMAD3_HUMAN	SMAD3	physical	21532621
EP300_HUMAN	EP300	physical	22033265
SP1_HUMAN	SP1	physical	22033265
DACH1_HUMAN	DACH1	physical	14525983
SKI_HUMAN	SKI	physical	14525983
UBP15_HUMAN	USP15	physical	22344298
HGS_HUMAN	HGS	physical	11094085
UBC9_HUMAN	UBE2I	physical	12621041
SMAD2_HUMAN	SMAD2	physical	12621041
HGS_HUMAN	HGS	physical	16516194
PAX6_HUMAN	PAX6	physical	17251190
SMAD3_HUMAN	SMAD3	physical	19768112
ZMIZ1_HUMAN	ZMIZ1	physical	16777850
SP1_HUMAN	SP1	physical	16714330
SMAD2_HUMAN	SMAD2	physical	15761153
SKIL_HUMAN	SKIL	physical	15761153
TGFR1_HUMAN	TGFBR1	physical	15761153
SMAD3_HUMAN	SMAD3	physical	15761153
SKI_HUMAN	SKI	physical	15761153
SMAD1_HUMAN	SMAD1	physical	15761153
SMAD2_HUMAN	SMAD2	physical	17591701
SMAD3_HUMAN	SMAD3	physical	17591701
HERC5_HUMAN	HERC5	physical	12202226
SMAD3_HUMAN	SMAD3	physical	10092624
SMAD4_HUMAN	SMAD4	physical	10092624
NOTC4_HUMAN	NOTCH4	physical	16007227
SMAD1_HUMAN	SMAD1	physical	9111321
SMAD2_HUMAN	SMAD2	physical	9111321
SMAD3_HUMAN	SMAD3	physical	9111321
SMAD4_HUMAN	SMAD4	physical	9111321
SMAD2_HUMAN	SMAD2	physical	15467747
PSD11_HUMAN	PSMD11	physical	15231748
MK13_HUMAN	MAPK13	physical	15231748
PR40A_HUMAN	PRPF40A	physical	15231748
PIAS1_HUMAN	PIAS1	physical	15231748
CSH1_HUMAN	CSH1	physical	15231748
CSH2_HUMAN	CSH1	physical	15231748
RU17_HUMAN	SNRNP70	physical	15231748
RALA_HUMAN	RALA	physical	15231748
PSG2_HUMAN	PSG2	physical	15231748
SKI_HUMAN	SKI	physical	15231748
SKIL_HUMAN	SKIL	physical	15231748
CD59_HUMAN	CD59	physical	15231748
MYOD1_HUMAN	MYOD1	physical	15231748
JUNB_HUMAN	JUNB	physical	15231748
RFX1_HUMAN	RFX1	physical	15231748
FBLN1_HUMAN	FBLN1	physical	15231748
DNJB2_HUMAN	DNAJB2	physical	15231748
RL28_HUMAN	RPL28	physical	15231748
TCTA_HUMAN	TCTA	physical	15231748
UBC9_HUMAN	UBE2I	physical	15231748
EF1A1_HUMAN	EEF1A1	physical	15231748
SMAD3_HUMAN	SMAD3	physical	15231748
VIGLN_HUMAN	HDLBP	physical	15231748
PSG9_HUMAN	PSG9	physical	15231748
TDG_HUMAN	TDG	physical	15231748
GPNMB_HUMAN	GPNMB	physical	15231748
SMAD2_HUMAN	SMAD2	physical	15231748
ZBED5_HUMAN	ZBED5	physical	15231748
MCAF1_HUMAN	ATF7IP	physical	15231748
NELFD_HUMAN	NELFCD	physical	15231748
DCP1B_HUMAN	DCP1B	physical	15231748
CNKR1_HUMAN	CNKSR1	physical	15231748
RMD5B_HUMAN	RMND5B	physical	15231748
UHRF2_HUMAN	UHRF2	physical	15231748
SMAD5_HUMAN	SMAD5	physical	15231748
TM9S2_HUMAN	TM9SF2	physical	15231748
USB1_HUMAN	USB1	physical	15231748
PAPP2_HUMAN	PAPPA2	physical	15231748
XPO5_HUMAN	XPO5	physical	15231748
HM20A_HUMAN	HMG20A	physical	15231748
DCP1A_HUMAN	DCP1A	physical	15231748
TEN3_HUMAN	TENM3	physical	15231748
ZMYM2_HUMAN	ZMYM2	physical	15231748
SPTB2_HUMAN	SPTBN1	physical	12543979
IRF7_HUMAN	IRF7	physical	14729983
IRF3_HUMAN	IRF3	physical	14729983
SKI_HUMAN	SKI	physical	12764135
SKIL_HUMAN	SKIL	physical	12764135
NCOR1_HUMAN	NCOR1	physical	12764135
FHL1_HUMAN	FHL1	physical	19139564
SMAD2_HUMAN	SMAD2	physical	19139564
SMAD3_HUMAN	SMAD3	physical	19139564
TGFI1_HUMAN	TGFB1I1	physical	15561701
UBC9_HUMAN	UBE2I	physical	21988832
SMAD4_HUMAN	SMAD4	physical	21988832
SOX12_HUMAN	SOX12	physical	21988832
S11IP_HUMAN	STK11IP	physical	21988832
CRYAB_HUMAN	CRYAB	physical	24307592
TRI33_HUMAN	TRIM33	physical	24307592
TRI33_HUMAN	TRIM33	physical	24382352
LMO4_HUMAN	LMO4	physical	25416956
RASF5_HUMAN	RASSF5	physical	25416956
FBW1A_HUMAN	BTRC	physical	25373906
DOK1_MOUSE	Dok1	physical	11927552
SMAD2_HUMAN	SMAD2	physical	11927552
SMAD3_HUMAN	SMAD3	physical	11927552
SMAD3_HUMAN	SMAD3	physical	15588252
GLYC_HUMAN	SHMT1	physical	26344197
NFIA_HUMAN	NFIA	physical	18215124
PARD3_HUMAN	PARD3	physical	12650946
BCAS3_HUMAN	BCAS3	physical	25640309
BEX1_HUMAN	BEX1	physical	25640309
DKK3_HUMAN	DKK3	physical	25640309
FA84B_HUMAN	FAM84B	physical	25640309
GREB1_HUMAN	GREB1	physical	25640309
IL24_HUMAN	IL24	physical	25640309
LYPD3_HUMAN	LYPD3	physical	25640309
S10AE_HUMAN	S100A14	physical	25640309
SPB5_HUMAN	SERPINB5	physical	25640309
THRSP_HUMAN	THRSP	physical	25640309
SKIL_HUMAN	SKIL	physical	25609649
SKI_HUMAN	SKI	physical	25609649
SMAD3_HUMAN	SMAD3	physical	25609649
SMAD2_HUMAN	SMAD2	physical	25609649
NFIX_HUMAN	NFIX	physical	25609649
NFKB1_HUMAN	NFKB1	physical	25609649
SMAD4_HUMAN	SMAD4	physical	25609649
SMAD9_HUMAN	SMAD9	physical	25609649
CAF1B_HUMAN	CHAF1B	physical	25609649
NKX25_HUMAN	NKX2-5	physical	25609649
DCP1A_HUMAN	DCP1A	physical	25609649
ZBT7A_HUMAN	ZBTB7A	physical	25514493
EP300_HUMAN	EP300	physical	25514493
CBP_HUMAN	CREBBP	physical	25514493
SMAD7_HUMAN	SMAD7	physical	26555259
WEE1_HUMAN	WEE1	genetic	28319113
CSN5_HUMAN	COPS5	physical	27060206
AHR_HUMAN	AHR	physical	27060206
USP9X_HUMAN	USP9X	physical	28115363
SMAD3_HUMAN	SMAD3	physical	28115363
TRI33_HUMAN	TRIM33	physical	28115363
UBP4_HUMAN	USP4	physical	28468752
SMUF2_HUMAN	SMURF2	physical	28468752

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
260350	Pancreatic cancer (PNCA)
174900	Juvenile polyposis syndrome (JPS)
175050	Juvenile polyposis/hereditary hemorrhagic telangiectasia syndrome (JP/HHT)
187300] in a single individual. JIP and HHT are autosomal dominant disorders with distinct and non-overlapping clinical features. The former, an inherited gastrointestinal malignancy predisposition, is caused by mutations in SMAD4 or BMPR1A, and the latter is a vascular malformation disorder caused by mutations in ENG or ACVRL1. All four genes encode proteins involved in the transforming-growth-factor-signaling pathway. Although there are reports of patients and families with phenotypes of both disorders combined, the genetic etiology of this association is unknown. {ECO
Colorectal cancer (CRC) [	DISEASE
	Note=SMAD4 variants may be associated with susceptibility to pulmonary hypertension, a disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs.
139210
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SMAD4_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-37; LYS-428 AND LYS-507, ANDMASS SPECTROMETRY.	19608861 [Abstract]

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