SMAD3_HUMAN - dbPTM
SMAD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAD3_HUMAN
UniProt AC P84022
Protein Name Mothers against decapentaplegic homolog 3
Gene Name SMAD3
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization Cytoplasm . Nucleus . Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 (PubMed:15799969). Through the action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex
Protein Description Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator..
Protein Sequence MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
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
2Acetylation------MSSILPFTP
------CCCCCCCCH
26.5322814378
2Phosphorylation------MSSILPFTP
------CCCCCCCCH
26.5329255136
3Phosphorylation-----MSSILPFTPP
-----CCCCCCCCHH
27.1829255136
8PhosphorylationMSSILPFTPPIVKRL
CCCCCCCCHHHHHHH
26.6429255136
13UbiquitinationPFTPPIVKRLLGWKK
CCCHHHHHHHHCCCC
37.74-
19AcetylationVKRLLGWKKGEQNGQ
HHHHHCCCCCCCCCC
49.4517074756
20AcetylationKRLLGWKKGEQNGQE
HHHHCCCCCCCCCCH
62.2617074756
29AcetylationEQNGQEEKWCEKAVK
CCCCCHHHHHHHHHH
57.2917478422
33AcetylationQEEKWCEKAVKSLVK
CHHHHHHHHHHHHHH
56.1725953088
33UbiquitinationQEEKWCEKAVKSLVK
CHHHHHHHHHHHHHH
56.17PubMed
36SumoylationKWCEKAVKSLVKKLK
HHHHHHHHHHHHHHH
42.82-
36AcetylationKWCEKAVKSLVKKLK
HHHHHHHHHHHHHHH
42.8225953088
36SumoylationKWCEKAVKSLVKKLK
HHHHHHHHHHHHHHH
42.82-
37PhosphorylationWCEKAVKSLVKKLKK
HHHHHHHHHHHHHHH
31.6224719451
45PhosphorylationLVKKLKKTGQLDELE
HHHHHHHHCCHHHHH
28.6825599653
53UbiquitinationGQLDELEKAITTQNV
CCHHHHHHHHHCCCC
58.68PubMed
63UbiquitinationTTQNVNTKCITIPRS
HCCCCCCEEEEEECC
20.59-
66PhosphorylationNVNTKCITIPRSLDG
CCCCEEEEEECCCCC
34.1124719451
78PhosphorylationLDGRLQVSHRKGLPH
CCCCEEEECCCCCCE
12.4726670566
81UbiquitinationRLQVSHRKGLPHVIY
CEEEECCCCCCEEEE
60.42PubMed
88PhosphorylationKGLPHVIYCRLWRWP
CCCCEEEEEEECCCC
3.14-
125PhosphorylationDEVCVNPYHYQRVET
CCEEECCCCCCCCCC
14.14-
132PhosphorylationYHYQRVETPVLPPVL
CCCCCCCCCCCCCCC
18.8130266825
179PhosphorylationPQSNIPETPPPGYLS
CCCCCCCCCCCCCCC
35.4219218245
183AcetylationIPETPPPGYLSEDGE
CCCCCCCCCCCCCCC
41.6119608861
204PhosphorylationNHSMDAGSPNLSPNP
CCCCCCCCCCCCCCC
16.6119218245
208PhosphorylationDAGSPNLSPNPMSPA
CCCCCCCCCCCCCCC
29.3014512875
213PhosphorylationNLSPNPMSPAHNNLD
CCCCCCCCCCCCCCC
21.8618032789
264PhosphorylationVDGFTDPSNSERFCL
ECCCCCCCCCHHHHH
56.66-
273AcetylationSERFCLGLLSNVNRN
CHHHHHHHHHCCCHH
2.8219608861
275PhosphorylationRFCLGLLSNVNRNAA
HHHHHHHHCCCHHHH
43.7221712546
286PhosphorylationRNAAVELTRRHIGRG
HHHHHHHHHHHCCCC
16.4929262532
309PhosphorylationEVFAECLSDSAIFVQ
HHHHHHHCCCEEEEE
40.97-
333AcetylationWHPATVCKIPPGCNL
CCCCCEEECCCCCCE
54.6425953088
334AcetylationHPATVCKIPPGCNLK
CCCCEEECCCCCCEE
4.1519608861
375PhosphorylationRMCTIRMSFVKGWGA
HHHHHHHHHHCCCCC
19.6222393057
378MalonylationTIRMSFVKGWGAEYR
HHHHHHHCCCCCCHH
47.1126320211
378AcetylationTIRMSFVKGWGAEYR
HHHHHHHCCCCCCHH
47.1119608861
388PhosphorylationGAEYRRQTVTSTPCW
CCCHHCEECCCCCEE
24.76-
412PhosphorylationQWLDKVLTQMGSPSI
HHHHHHHHHCCCCCC
21.3529396449
416PhosphorylationKVLTQMGSPSIRCSS
HHHHHCCCCCCCCCC
15.3325159151
418PhosphorylationLTQMGSPSIRCSSVS
HHHCCCCCCCCCCCC
25.1021712546
422PhosphorylationGSPSIRCSSVS----
CCCCCCCCCCC----
24.7525056879
423PhosphorylationSPSIRCSSVS-----
CCCCCCCCCC-----
29.979380693
425PhosphorylationSIRCSSVS-------
CCCCCCCC-------
36.139380693

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
8TPhosphorylationKinaseCDK2P24941
Uniprot
8TPhosphorylationKinaseCDK4P30285
PSP
8TPhosphorylationKinaseCDK2P97377
PSP
8TPhosphorylationKinaseCDK4P11802
Uniprot
179TPhosphorylationKinaseCDK9P50750
PSP
179TPhosphorylationKinaseCDK8P49336
PSP
179TPhosphorylationKinaseCDK4P30285
PSP
179TPhosphorylationKinaseMAPK1P28482
GPS
179TPhosphorylationKinaseMAPK-Uniprot
179TPhosphorylationKinaseCDK4P11802
Uniprot
179TPhosphorylationKinaseCDK2P97377
PSP
179TPhosphorylationKinaseAKT1P31749
PSP
179TPhosphorylationKinaseCDK2P24941
Uniprot
204SPhosphorylationKinaseMAPK-Uniprot
204SPhosphorylationKinaseMAPK1P28482
GPS
204SPhosphorylationKinaseMELKQ61846
PSP
204SPhosphorylationKinaseGSK3-Uniprot
204SPhosphorylationKinaseCDK4P11802
PSP
208SPhosphorylationKinaseMAPK-Uniprot
208SPhosphorylationKinaseCDK9P50750
PSP
208SPhosphorylationKinaseMAPK1P28482
GPS
208SPhosphorylationKinaseCDK4P11802
PSP
208SPhosphorylationKinaseCDK8P49336
PSP
213SPhosphorylationKinaseMAPK1P28482
GPS
213SPhosphorylationKinaseCDK2P24941
Uniprot
213SPhosphorylationKinaseCDK2P97377
PSP
213SPhosphorylationKinaseCDK4P11802
Uniprot
213SPhosphorylationKinaseCDK4P30285
PSP
213SPhosphorylationKinaseCDK9P50750
PSP
213SPhosphorylationKinaseCDK8P49336
PSP
418SPhosphorylationKinaseCK1G2P78368
PSP
418SPhosphorylationKinaseCK1-Uniprot
422SPhosphorylationKinaseTGFBR1P36897
Uniprot
423SPhosphorylationKinaseTGFBR1P36897
Uniprot
425SPhosphorylationKinaseTGFBR1P36897
Uniprot
-KUbiquitinationE3 ubiquitin ligaseWWP2O00308
PMID:21258410
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:19917253
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:15781469
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:11359933
-KUbiquitinationE3 ubiquitin ligasePJA1Q8NG27
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseRNF111Q6ZNA4
PMID:18950738
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:15108358

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
179TPhosphorylation

15241418
204SPhosphorylation

15241418
208SPhosphorylation

15241418
208SPhosphorylation

15241418
418SPhosphorylation

18794808
418Subiquitylation

18794808

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 SMAD3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRAS2_MOUSERras2physical
15761153
ARHG7_MOUSEArhgef7physical
15761153
2ABD_MOUSEPpp2r2dphysical
15761153
WWP2_MOUSEWwp2physical
15761153
RHES_MOUSERasd2physical
15761153
RAB38_MOUSERab38physical
15761153
FBX3_MOUSEFbxo3physical
15761153
SQSTM_MOUSESqstm1physical
15761153
MP2K3_MOUSEMap2k3physical
15761153
WEE1_MOUSEWee1physical
15761153
ARHG6_MOUSEArhgef6physical
15761153
RGS3_MOUSERgs3physical
15761153
TRI35_MOUSETrim35physical
15761153
CLASR_MOUSEClasrpphysical
15761153
SMAD2_MOUSESmad2physical
15761153
SMAD3_MOUSESmad3physical
15761153
GSC_MOUSEGscphysical
15761153
ANDR_HUMANARphysical
11280774
ANDR_HUMANARphysical
11707452
PML_HUMANPMLphysical
15356634
ZFYV9_HUMANZFYVE9physical
15356634
APC10_HUMANANAPC10physical
15144564
CASL_HUMANNEDD9physical
15144564
FOXO1_HUMANFOXO1physical
15084259
FOXO4_HUMANFOXO4physical
15084259
FOXO3_HUMANFOXO3physical
15084259
SMAD4_HUMANSMAD4physical
15084259
FBW1A_HUMANBTRCphysical
14988407
PIAS3_HUMANPIAS3physical
14691252
NOTC1_HUMANNOTCH1physical
14638857
EID2_HUMANEID2physical
14612439
GCR_HUMANNR3C1physical
12902338
SKI_HUMANSKIphysical
12874272
HIPK2_HUMANHIPK2physical
12874272
SKI_HUMANSKIphysical
12857746
ATF3_HUMANATF3physical
12718878
DVL1_HUMANDVL1physical
12650946
ERBIN_HUMANERBB2IPphysical
12650946
ATF2_HUMANATF2physical
10085140
SKIL_HUMANSKILphysical
11691834
CDC27_HUMANCDC27physical
11691834
CDC16_HUMANCDC16physical
11691834
DAB2_HUMANDAB2physical
11387212
JUN_HUMANJUNphysical
9732876
FOS_HUMANFOSphysical
9732876
SMAD4_HUMANSMAD4physical
12419246
IMB1_HUMANKPNB1physical
10846168
RBL1_HUMANRBL1physical
12150994
E2F4_HUMANE2F4physical
12150994
JUN_HUMANJUNphysical
10903323
CTNB1_HUMANCTNNB1physical
12000714
SKIL_HUMANSKILphysical
10531062
RUNX2_HUMANRUNX2physical
10962029
TFE3_HUMANTFE3physical
12551947
MAX_HUMANMAXphysical
12551947
SMUF2_HUMANSMURF2physical
11016919
AKT1_HUMANAKT1physical
16362038
SMAD2_HUMANSMAD2physical
9311995
SMAD4_HUMANSMAD4physical
9311995
MEN1_HUMANMEN1physical
11274402
NFYC_HUMANNFYCphysical
12023901
ANDR_HUMANARphysical
12226080
JUNB_HUMANJUNBphysical
10220381
JUN_HUMANJUNphysical
10220381
JUND_HUMANJUNDphysical
10220381
RUNX1_HUMANRUNX1physical
10531362
RUNX2_HUMANRUNX2physical
10531362
RUNX3_HUMANRUNX3physical
10531362
SNW1_HUMANSNW1physical
11278756
STRAP_HUMANSTRAPphysical
10757800
SMAD4_HUMANSMAD4physical
9892009
SMAD7_HUMANSMAD7genetic
9892009
CASL_HUMANNEDD9physical
11118211
SMAD4_HUMANSMAD4physical
11114293
SP1_HUMANSP1physical
11114293
CEBPA_HUMANCEBPAphysical
12524424
CEBPB_HUMANCEBPBphysical
12524424
CEBPD_HUMANCEBPDphysical
12524424
PIN1_HUMANPIN1physical
19122240
RN111_HUMANRNF111physical
18950738
KC1G2_HUMANCSNK1G2physical
18794808
GSK3B_HUMANGSK3Bphysical
18172167
KDM5C_HUMANKDM5Cphysical
18078810
SMAD4_HUMANSMAD4physical
20142324
BMP7_HUMANBMP7physical
20093492
UCHL5_HUMANUCHL5physical
16027725
BPTF_HUMANBPTFphysical
18974875
MPIP1_HUMANCDC25Aphysical
15798217
CUL1_HUMANCUL1physical
15798217
CREST_HUMANSS18L1physical
20211142
ZBTB3_HUMANZBTB3physical
20211142
NEDD4_HUMANNEDD4physical
15496141
CITE2_HUMANCITED2physical
16619037
WWP1_HUMANWWP1physical
15221015
SMUF1_HUMANSMURF1physical
15221015
SMUF2_HUMANSMURF2physical
15221015
GRIP1_HUMANGRIP1physical
16423881
PIAS4_HUMANPIAS4physical
12904571
MYCD_HUMANMYOCDphysical
16224064
TYY1_HUMANYY1physical
12808092
SKI_HUMANSKIphysical
12732634
SMAD4_HUMANSMAD4physical
12732634
MED15_HUMANMED15physical
12167862
MED24_HUMANMED24physical
12167862
MED6_HUMANMED6physical
12167862
SMAD4_HUMANSMAD4physical
12167862
KAT2B_HUMANKAT2Bphysical
15994459
HDAC5_HUMANHDAC5physical
15990875
HDAC4_HUMANHDAC4physical
15990875
EVI1_HUMANMECOMphysical
15849193
CBP_HUMANCREBBPphysical
15849193
BRCA1_HUMANBRCA1physical
15735739
SOX9_HUMANSOX9physical
15623506
PITX1_HUMANPITX1physical
18339718
PITX2_HUMANPITX2physical
18339718
HDAC1_HUMANHDAC1physical
11306568
SKI_HUMANSKIphysical
11306568
SKIL_HUMANSKILphysical
11306568
TGIF1_HUMANTGIF1physical
11306568
SIN3A_HUMANSIN3Aphysical
11306568
JUN_HUMANJUNphysical
11306568
KAT2B_HUMANKAT2Bphysical
11058129
EP300_HUMANEP300physical
11058129
EP300_HUMANEP300physical
10575014
SKI_HUMANSKIphysical
10575014
HDAC1_HUMANHDAC1physical
10575014
SIN3A_MOUSESin3aphysical
10575014
EP300_HUMANEP300physical
15133024
VDR_HUMANVDRphysical
10037600
KAT2A_HUMANKAT2Aphysical
15009097
KAT2B_HUMANKAT2Bphysical
15009097
CBP_HUMANCREBBPphysical
18003620
SMRC2_HUMANSMARCC2physical
18003620
ARI1A_HUMANARID1Aphysical
18003620
SMRC1_HUMANSMARCC1physical
18003620
SMCA4_HUMANSMARCA4physical
18003620
ERBIN_HUMANERBB2IPphysical
18003620
TRI33_HUMANTRIM33physical
18003620
NCOA3_HUMANNCOA3physical
18003620
RBX1_HUMANRBX1physical
11359933
SMUF2_HUMANSMURF2physical
11158580
CTCF_HUMANCTCFphysical
20427289
CTNB1_HUMANCTNNB1physical
20571128
SMAD4_HUMANSMAD4physical
20564330
EP300_HUMANEP300physical
20564330
ATF3_HUMANATF3physical
20930144
ESR1_HUMANESR1physical
20207742
SRY_HUMANSRYphysical
15527767
ACTB_HUMANACTBphysical
15527767
PRTN3_HUMANPRTN3physical
15527767
SRBP2_HUMANSREBF2physical
15527767
SMAD4_HUMANSMAD4physical
22045334
CHIP_HUMANSTUB1physical
14701756
WWP2_HUMANWWP2physical
21258410
CBP_HUMANCREBBPphysical
15750622
FOXH1_HUMANFOXH1physical
15750622
LEF1_HUMANLEF1physical
15750622
CTNB1_HUMANCTNNB1physical
21965288
USP9X_HUMANUSP9Xphysical
19135894
SMAD4_HUMANSMAD4physical
19135894
EP300_HUMANEP300physical
9679056
SP1_HUMANSP1physical
10878024
HNF4A_HUMANHNF4Aphysical
10995777
SKI_HUMANSKIphysical
12426322
SKIL_HUMANSKILphysical
12426322
NU214_HUMANNUP214physical
12917407
NU153_HUMANNUP153physical
12917407
SMAD4_HUMANSMAD4physical
12917407
UBP15_HUMANUSP15physical
21947082
CTNB1_HUMANCTNNB1physical
22241478
YAP1_HUMANYAP1physical
19914168
SKI_HUMANSKIphysical
17283070
CBP_HUMANCREBBPphysical
17283070
SMAD4_HUMANSMAD4physical
17283070
EPAS1_HUMANEPAS1physical
21057546
RGCC_HUMANRGCCphysical
21990365
SUV91_HUMANSUV39H1physical
21862595
CBL_HUMANCBLphysical
22310290
SMAD4_HUMANSMAD4physical
22310290
ZEB2_HUMANZEB2physical
16061479
PIN1_HUMANPIN1physical
21685363
NEDD4_HUMANNEDD4physical
21685363
NED4L_HUMANNEDD4Lphysical
19917253
SMAD4_HUMANSMAD4physical
19917253
TRIB3_HUMANTRIB3physical
21896644
UBP15_HUMANUSP15physical
22344298
HGS_HUMANHGSphysical
11094085
NED4L_HUMANNEDD4Lphysical
22921829
PAX6_HUMANPAX6physical
17251190
BRCA1_HUMANBRCA1physical
19768112
SMAD4_HUMANSMAD4physical
19768112
ZMIZ1_HUMANZMIZ1physical
16777850
SMAD4_HUMANSMAD4physical
18729074
SMAD2_HUMANSMAD2physical
18729074
KC1D_HUMANCSNK1Dphysical
18729074
DDX3Y_HUMANDDX3Yphysical
18729074
ERBIN_HUMANERBB2IPphysical
18729074
MK01_HUMANMAPK1physical
18729074
HSP74_HUMANHSPA4physical
18729074
MAN1_HUMANLEMD3physical
18729074
PJA1_HUMANPJA1physical
18729074
ZFYV9_HUMANZFYVE9physical
18729074
SNW1_HUMANSNW1physical
18729074
SMUF2_HUMANSMURF2physical
18729074
WWP2_HUMANWWP2physical
18729074
TYY1_HUMANYY1physical
18729074
RL3_HUMANRPL3physical
18729074
ATX2L_HUMANATXN2Lphysical
18729074
FA83G_HUMANFAM83Gphysical
18729074
CHD8_HUMANCHD8physical
18729074
CMC1_HUMANSLC25A12physical
18729074
NHRF2_HUMANSLC9A3R2physical
18729074
LRCH1_HUMANLRCH1physical
18729074
YTHD2_HUMANYTHDF2physical
18729074
TCPA_HUMANTCP1physical
18729074
E41L5_HUMANEPB41L5physical
18729074
PTN6_HUMANPTPN6physical
18729074
DOCK9_HUMANDOCK9physical
18729074
PSPC1_HUMANPSPC1physical
18729074
DDX4_HUMANDDX4physical
18729074
DDX3X_HUMANDDX3Xphysical
18729074
DNJA2_HUMANDNAJA2physical
18729074
SIK3_HUMANSIK3physical
18729074
U2AF2_HUMANU2AF2physical
18729074
DHX8_HUMANDHX8physical
18729074
SARG_HUMANC1orf116physical
18729074
ITB4_HUMANITGB4physical
18729074
CD11A_HUMANCDK11Aphysical
18729074
RFIP5_HUMANRAB11FIP5physical
18729074
SMAD1_HUMANSMAD1physical
18729074
IRS1_HUMANIRS1physical
18729074
SMAD5_HUMANSMAD5physical
18729074
DYR1A_HUMANDYRK1Aphysical
18729074
BUB3_HUMANBUB3physical
18729074
SQOR_HUMANSQRDLphysical
18729074
PABP1_HUMANPABPC1physical
18729074
DCAF7_HUMANDCAF7physical
18729074
OPA1_HUMANOPA1physical
18729074
VAV2_HUMANVAV2physical
18729074
UBP7_HUMANUSP7physical
18729074
RL4_HUMANRPL4physical
18729074
TGFR1_HUMANTGFBR1physical
19758997
SP1_HUMANSP1physical
16714330
SMAD4_HUMANSMAD4physical
15922743
S10A4_HUMANS100A4physical
20070253
ERBIN_HUMANERBB2IPphysical
17591701
SMAD4_HUMANSMAD4physical
17591701
IKKA_HUMANCHUKphysical
18268325
A4_HUMANAPPphysical
21832049
SMAD4_HUMANSMAD4physical
15350224
SMAD4_HUMANSMAD4physical
10092624
SMAD3_HUMANSMAD3physical
10092624
PIN1_HUMANPIN1physical
19920136
HIF1A_HUMANHIF1Aphysical
11486006
RNZ2_HUMANELAC2physical
16636667
NOTC4_HUMANNOTCH4physical
16007227
SMAD1_HUMANSMAD1physical
9111321
SMAD2_HUMANSMAD2physical
9111321
SMAD3_HUMANSMAD3physical
9111321
SMAD4_HUMANSMAD4physical
9111321
SMAD4_HUMANSMAD4physical
15467747
PSD11_HUMANPSMD11physical
15231748
ZEB2_HUMANZEB2physical
15231748
GANP_HUMANMCM3APphysical
15231748
ZFYV9_HUMANZFYVE9physical
15231748
CP11A_HUMANCYP11A1physical
15231748
RLA0_HUMANRPLP0physical
15231748
RU17_HUMANSNRNP70physical
15231748
XRCC6_HUMANXRCC6physical
15231748
ZEP1_HUMANHIVEP1physical
15231748
FLNA_HUMANFLNAphysical
15231748
TGM2_HUMANTGM2physical
15231748
2AAA_HUMANPPP2R1Aphysical
15231748
ZNF83_HUMANZNF83physical
15231748
ZBT16_HUMANZBTB16physical
15231748
PCDH1_HUMANPCDH1physical
15231748
PAPP1_HUMANPAPPAphysical
15231748
TMED1_HUMANTMED1physical
15231748
ANK3_HUMANANK3physical
15231748
SMAD4_HUMANSMAD4physical
15231748
IL27B_HUMANEBI3physical
15231748
NCOA6_HUMANNCOA6physical
15231748
PLAG1_HUMANPLAG1physical
15231748
CXXC5_HUMANCXXC5physical
15231748
KANL1_HUMANKANSL1physical
15231748
ZN329_HUMANZNF329physical
15231748
GGA1_HUMANGGA1physical
15231748
SVEP1_HUMANSVEP1physical
15231748
RANB9_HUMANRANBP9physical
15231748
EPAS1_HUMANEPAS1physical
15231748
SP130_HUMANSAP130physical
15231748
VISTA_HUMANC10orf54physical
15231748
SMUF1_HUMANSMURF1physical
15231748
HEYL_HUMANHEYLphysical
15231748
CFDP1_HUMANCFDP1physical
15231748
SIA7B_HUMANST6GALNAC2physical
15231748
PRDM4_HUMANPRDM4physical
15231748
PLAL1_HUMANPLAGL1physical
15231748
KMT2B_HUMANKMT2Bphysical
15231748
KDM2A_HUMANKDM2Aphysical
15231748
MTF2_HUMANMTF2physical
15231748
HEY1_HUMANHEY1physical
15231748
GMEB1_HUMANGMEB1physical
15231748
TGFR1_HUMANTGFBR1physical
12543979
SMAD2_HUMANSMAD2physical
12543979
SMAD4_HUMANSMAD4physical
12543979
SPTB2_HUMANSPTBN1physical
12543979
SMAD3_HUMANSMAD3physical
12154125
ZFYV9_HUMANZFYVE9physical
12154125
SKI_HUMANSKIphysical
12154125
DEDD_HUMANDEDDphysical
20553715
SH22A_HUMANSH2D2Aphysical
16806069
IRF7_HUMANIRF7physical
14729983
TSC2_HUMANTSC2physical
15066998
FHL1_HUMANFHL1physical
19139564
RUNX1_HUMANRUNX1physical
15897867
TGFI1_HUMANTGFB1I1physical
15561701
SMAD4_HUMANSMAD4physical
23788427
SQSTM_HUMANSQSTM1physical
21988832
ZC12A_HUMANZC3H12Aphysical
21988832
T22D4_HUMANTSC22D4physical
21988832
ZMY11_HUMANZMYND11physical
21988832
UBQL4_HUMANUBQLN4physical
21988832
TYDP2_HUMANTDP2physical
21988832
TRFE_HUMANTFphysical
21988832
SMAD4_HUMANSMAD4physical
21988832
TLR4_HUMANTLR4physical
21988832
UBP7_HUMANUSP7physical
21988832
TANK_HUMANTANKphysical
21988832
ZCH14_HUMANZCCHC14physical
21988832
P63_HUMANTP63physical
23687300
TRI62_HUMANTRIM62physical
23838884
SMUF2_HUMANSMURF2physical
23973329
FOXM1_HUMANFOXM1physical
24382352
SMAD4_HUMANSMAD4physical
24382352
TRI33_HUMANTRIM33physical
24382352
FOXO3_HUMANFOXO3physical
24920680
MAFK_HUMANMAFKphysical
23737527
BACH1_HUMANBACH1physical
23737527
SMAD4_HUMANSMAD4physical
24157709
MEOX2_HUMANMEOX2physical
25416956
GO45_HUMANBLZF1physical
25416956
WWP1_HUMANWWP1physical
25416956
CPSF7_HUMANCPSF7physical
25416956
CCD33_HUMANCCDC33physical
25416956
TEKT4_HUMANTEKT4physical
25416956
EP300_HUMANEP300physical
16109717
EP300_HUMANEP300physical
12743039
CBP_HUMANCREBBPphysical
19589780
EP300_HUMANEP300physical
21567395
EP300_HUMANEP300physical
17469184
SKI_HUMANSKIphysical
17469184
SKIL_HUMANSKILphysical
17469184
DDX5_HUMANDDX5physical
19917253
IF4B_HUMANEIF4Bphysical
19917253
MAN1_HUMANLEMD3physical
19917253
XPO6_HUMANXPO6physical
19917253
TRI33_HUMANTRIM33physical
19917253
DOK1_MOUSEDok1physical
11927552
SMAD4_HUMANSMAD4physical
11927552
ZFYV9_HUMANZFYVE9physical
26186194
MAN1_HUMANLEMD3physical
26186194
SMAD9_HUMANSMAD9physical
26186194
SMAD2_HUMANSMAD2physical
26186194
LACRT_HUMANLACRTphysical
26186194
STRAP_HUMANSTRAPgenetic
10757800
NFIA_HUMANNFIAphysical
18215124
NCOA1_HUMANNCOA1physical
16423881
ERBIN_MOUSEErbb2ipphysical
12650946
PARD3_MOUSEPard3physical
12650946
DVL1_MOUSEDvl1physical
12650946
PARD3_HUMANPARD3physical
12650946
SMAD4_HUMANSMAD4physical
24584437
KAT2B_HUMANKAT2Bphysical
22995475
SMAD4_HUMANSMAD4physical
25514493
SMAD7_HUMANSMAD7physical
26555259
SMAD4_HUMANSMAD4physical
26555259
NED4L_HUMANNEDD4Lphysical
26555259
UCHL5_HUMANUCHL5physical
27604640
SMAD4_HUMANSMAD4physical
28115363
SMAD2_HUMANSMAD2physical
28514442
SMAD9_HUMANSMAD9physical
28514442
ZFYV9_HUMANZFYVE9physical
28514442
MAN1_HUMANLEMD3physical
28514442
LACRT_HUMANLACRTphysical
28514442
SMUF1_HUMANSMURF1physical
28839186
SMUF2_HUMANSMURF2physical
28881580

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
114500Colorectal cancer (CRC)
613795Loeys-Dietz syndrome 3 (LDS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMAD3_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-378, AND MASS SPECTROMETRY.
"Smad3 is acetylated by p300/CBP to regulate its transactivationactivity.";
Inoue Y., Itoh Y., Abe K., Okamoto T., Daitoku H., Fukamizu A.,Onozaki K., Hayashi H.;
Oncogene 26:500-508(2007).
Cited for: ACETYLATION AT LYS-378, FUNCTION, AND MUTAGENESIS OF LYS-333; LYS-341;LYS-378; LYS-409 AND 422-SER--SER-425.
Phosphorylation
ReferencePubMed
"Transforming growth factor-{beta}-inducible phosphorylation ofSmad3.";
Wang G., Matsuura I., He D., Liu F.;
J. Biol. Chem. 284:9663-9673(2009).
Cited for: PHOSPHORYLATION AT THR-179; SER-204 AND SER-208, SUBCELLULAR LOCATION,FUNCTION, AND MUTAGENESIS OF THR-179; SER-204 AND SER-208.
"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-416, AND MASSSPECTROMETRY.
"Ligand-dependent ubiquitination of Smad3 is regulated by caseinkinase 1 gamma 2, an inhibitor of TGF-beta signaling.";
Guo X., Waddell D.S., Wang W., Wang Z., Liberati N.T., Yong S.,Liu X., Wang X.-F.;
Oncogene 27:7235-7247(2008).
Cited for: INTERACTION WITH CSNK1G2, UBIQUITINATION, PHOSPHORYLATION AT SER-418BY CSNK1G2/CK1, AND MUTAGENESIS OF SER-418.
"Identification and characterization of ERK MAP kinase phosphorylationsites in Smad3.";
Matsuura I., Wang G., He D., Liu F.;
Biochemistry 44:12546-12553(2005).
Cited for: PHOSPHORYLATION AT THR-179; SER-204 AND SER-208, SUBCELLULAR LOCATION,FUNCTION, AND MUTAGENESIS OF THR-179; SER-204 AND SER-208.
"Cyclin-dependent kinases regulate the antiproliferative function ofSmads.";
Matsuura I., Denissova N.G., Wang G., He D., Long J., Liu F.;
Nature 430:226-231(2004).
Cited for: PHOSPHORYLATION AT THR-8; THR-179; SER-204; SER-208 AND SER-213,FUNCTION, AND MUTAGENESIS OF THR-8; THR-179; SER-204; SER-208 ANDSER-213.
"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 THR-8, AND MASSSPECTROMETRY.

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