SMAD2_HUMAN - dbPTM
SMAD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAD2_HUMAN
UniProt AC Q15796
Protein Name Mothers against decapentaplegic homolog 2
Gene Name SMAD2
Organism Homo sapiens (Human).
Sequence Length 467
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:9865696). On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, a
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 SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator..
Protein Sequence MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTPNTIDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
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
26.5320068231
2Phosphorylation------MSSILPFTP
------CCCCCCCCH
26.5319413330
3Phosphorylation-----MSSILPFTPP
-----CCCCCCCCHH
27.1825159151
8PhosphorylationMSSILPFTPPVVKRL
CCCCCCCCHHHHHHH
25.4129255136
13UbiquitinationPFTPPVVKRLLGWKK
CCCHHHHHHHHCCCC
37.25-
19AcetylationVKRLLGWKKSAGGSG
HHHHHCCCCCCCCCC
34.7417074756
20AcetylationKRLLGWKKSAGGSGG
HHHHCCCCCCCCCCC
38.7417074756
21PhosphorylationRLLGWKKSAGGSGGA
HHHCCCCCCCCCCCC
28.5528985074
39AcetylationEQNGQEEKWCEKAVK
CCCCCHHHHHHHHHH
57.29150215
46SumoylationKWCEKAVKSLVKKLK
HHHHHHHHHHHHHHH
42.82-
46SumoylationKWCEKAVKSLVKKLK
HHHHHHHHHHHHHHH
42.82-
47PhosphorylationWCEKAVKSLVKKLKK
HHHHHHHHHHHHHHH
31.6224719451
54UbiquitinationSLVKKLKKTGRLDEL
HHHHHHHHHCCHHHH
67.65-
63UbiquitinationGRLDELEKAITTQNC
CCHHHHHHHHHHCCC
58.68-
102PhosphorylationQWDTTGLYSFSEQTR
CCCCCCCEECCHHHC
14.7122817900
110PhosphorylationSFSEQTRSLDGRLQV
ECCHHHCCCCCCEEE
33.9111027280
118PhosphorylationLDGRLQVSHRKGLPH
CCCCEEEECCCCCCE
12.4724719451
121UbiquitinationRLQVSHRKGLPHVIY
CEEEECCCCCCEEEE
60.42-
121MalonylationRLQVSHRKGLPHVIY
CEEEECCCCCCEEEE
60.4226320211
128PhosphorylationKGLPHVIYCRLWRWP
CCCCEEEEEEECCCC
3.14-
151PhosphorylationKAIENCEYAFNLKKD
HHHHCCCEEEECCCC
20.7727642862
156UbiquitinationCEYAFNLKKDEVCVN
CCEEEECCCCCEEEC
60.32-
156SumoylationCEYAFNLKKDEVCVN
CCEEEECCCCCEEEC
60.32-
156SumoylationCEYAFNLKKDEVCVN
CCEEEECCCCCEEEC
60.32-
156AcetylationCEYAFNLKKDEVCVN
CCEEEECCCCCEEEC
60.3225953088
157UbiquitinationEYAFNLKKDEVCVNP
CEEEECCCCCEEECC
63.39-
165PhosphorylationDEVCVNPYHYQRVET
CCEEECCCCCCCCCC
14.1427642862
167PhosphorylationVCVNPYHYQRVETPV
EEECCCCCCCCCCCC
7.6827642862
172PhosphorylationYHYQRVETPVLPPVL
CCCCCCCCCCCCCCC
18.8130266825
197PhosphorylationLPPLDDYTHSIPENT
CCCCCCCCCCCCCCC
19.0116121194
220PhosphorylationQSNYIPETPPPGYIS
CCCCCCCCCCCCCCC
35.4219917253
240PhosphorylationSDQQLNQSMDTGSPA
CHHHHHHHCCCCCCC
19.9711027280
243PhosphorylationQLNQSMDTGSPAELS
HHHHHCCCCCCCCCC
30.8026074081
245PhosphorylationNQSMDTGSPAELSPT
HHHCCCCCCCCCCCC
24.0311027280
250PhosphorylationTGSPAELSPTTLSPV
CCCCCCCCCCCCCCC
16.2311027280
252PhosphorylationSPAELSPTTLSPVNH
CCCCCCCCCCCCCCC
36.6726074081
253PhosphorylationPAELSPTTLSPVNHS
CCCCCCCCCCCCCCC
28.7326074081
255PhosphorylationELSPTTLSPVNHSLD
CCCCCCCCCCCCCCC
25.3911027280
260PhosphorylationTLSPVNHSLDLQPVT
CCCCCCCCCCCCCCC
20.5511027280
317PhosphorylationRFCLGLLSNVNRNAT
CHHHHHHHCCCCCCC
43.7221712546
324PhosphorylationSNVNRNATVEMTRRH
HCCCCCCCHHHHHHH
22.13-
351PhosphorylationEVFAECLSDSAIFVQ
HHHHHHHCCCEEEEE
40.97-
417PhosphorylationRMCTIRMSFVKGWGA
HHHHHHHHHHCCCCC
19.6222393057
420MalonylationTIRMSFVKGWGAEYR
HHHHHHHCCCCCCHH
47.1126320211
420AcetylationTIRMSFVKGWGAEYR
HHHHHHHCCCCCCHH
47.1122634611
430PhosphorylationGAEYRRQTVTSTPCW
CCCHHCEECCCCCEE
24.76-
454PhosphorylationQWLDKVLTQMGSPSV
HHHHHHHHHCCCCCC
21.3528450419
458PhosphorylationKVLTQMGSPSVRCSS
HHHHHCCCCCCCCCC
14.5225159151
460PhosphorylationLTQMGSPSVRCSSMS
HHHCCCCCCCCCCCC
24.7222115753
464PhosphorylationGSPSVRCSSMS----
CCCCCCCCCCC----
20.649892009
465PhosphorylationSPSVRCSSMS-----
CCCCCCCCCC-----
27.0321996745
467PhosphorylationSVRCSSMS-------
CCCCCCCC-------
38.7321996745

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
8TPhosphorylationKinaseMK03P27361
PhosphoELM
110SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
197TPhosphorylationKinaseGRK2P25098
PSP
220TPhosphorylationKinaseMAPK3P27361
GPS
220TPhosphorylationKinaseMAPK1P28482
GPS
240SPhosphorylationKinaseCAMK2-Uniprot
240SPhosphorylationKinaseCAMK2-FAMILY-GPS
240SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
245SPhosphorylationKinaseMAPK3P27361
GPS
245SPhosphorylationKinaseMAPK1P28482
GPS
245SPhosphorylationKinaseMELKQ61846
PSP
250SPhosphorylationKinaseMAPK3P27361
GPS
250SPhosphorylationKinaseMAPK1P28482
GPS
255SPhosphorylationKinaseMAPK1P28482
GPS
255SPhosphorylationKinaseMAPK3P27361
GPS
260SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
417SPhosphorylationKinasePAK2Q13177
PSP
464SPhosphorylationKinaseBMR1BO00238
PhosphoELM
464SPhosphorylationKinaseTGFR1P36897
PhosphoELM
464SPhosphorylationKinasePAK2Q13177
PSP
465SPhosphorylationKinasePAK2Q13177
PSP
465SPhosphorylationKinaseTGFR1P36897
PhosphoELM
465SPhosphorylationKinaseBMR1BO00238
PhosphoELM
467SPhosphorylationKinasePAK2Q13177
PSP
467SPhosphorylationKinaseTGFR1P36897
PhosphoELM
467SPhosphorylationKinaseBMR1BO00238
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:11016919
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:15496141
-KUbiquitinationE3 ubiquitin ligaseWWP1Q9H0M0
PMID:15359284
-KUbiquitinationE3 ubiquitin ligaseRNF111Q6ZNA4
PMID:18950738

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
19KAcetylation

17074756
220TPhosphorylation

12193595
240SPhosphorylation

11879191
245SPhosphorylation

12193595
250SPhosphorylation

12193595
255SPhosphorylation

12193595
465/467SPhosphorylation

8980228
465/467SPhosphorylation

8980228
465/467SPhosphorylation

8980228

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 SMAD2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHES_MOUSERasd2physical
15761153
RAB34_MOUSERab34physical
15761153
REBL1_MOUSERhebl1physical
15761153
RAB38_MOUSERab38physical
15761153
RHBT1_MOUSERhobtb1physical
15761153
ARHG7_MOUSEArhgef7physical
15761153
RS27A_MOUSERps27aphysical
15761153
FBX3_MOUSEFbxo3physical
15761153
SQSTM_MOUSESqstm1physical
15761153
2ABD_MOUSEPpp2r2dphysical
15761153
MP2K3_MOUSEMap2k3physical
15761153
NUAK2_MOUSENuak2physical
15761153
UHMK1_MOUSEUhmk1physical
15761153
ARHG6_MOUSEArhgef6physical
15761153
RGS3_MOUSERgs3physical
15761153
LHX9_MOUSELhx9physical
15761153
TRI35_MOUSETrim35physical
15761153
WWP2_MOUSEWwp2physical
15761153
RHOJ_MOUSERhojphysical
15761153
RHOD_MOUSERhodphysical
15761153
ARL4D_MOUSEArl4dphysical
15761153
ARHG1_MOUSEArhgef1physical
15761153
PRP17_MOUSECdc40physical
15761153
IRAK2_MOUSEIrak2physical
15761153
RBTN2_MOUSELmo2physical
15761153
SMAD2_MOUSESmad2physical
15761153
SMAD3_MOUSESmad3physical
15761153
ZFYV9_HUMANZFYVE9physical
15356634
APC10_HUMANANAPC10physical
15144564
PIAS3_HUMANPIAS3physical
14691252
EID2_HUMANEID2physical
14612439
HIPK2_HUMANHIPK2physical
12874272
SKI_HUMANSKIphysical
12874272
DVL1_HUMANDVL1physical
12650946
ERBIN_HUMANERBB2IPphysical
12650946
TGIF1_HUMANTGIF1physical
10199400
SMAD4_HUMANSMAD4physical
10199400
HDAC1_HUMANHDAC1physical
10199400
SMAD4_HUMANSMAD4physical
11264182
SNIP1_HUMANSNIP1physical
10887155
EP300_HUMANEP300physical
11371641
TGIF1_HUMANTGIF1physical
11371641
JUN_HUMANJUNphysical
11371641
CDC27_HUMANCDC27physical
11691834
CDC16_HUMANCDC16physical
11691834
DAB2_HUMANDAB2physical
11387212
SMAD4_HUMANSMAD4physical
12419246
CTNB1_HUMANCTNNB1physical
12000714
MEF2A_HUMANMEF2Aphysical
11160896
MEF2C_HUMANMEF2Cphysical
11160896
SKIL_HUMANSKILphysical
10531062
SKI_HUMANSKIphysical
10485843
SMUF2_HUMANSMURF2physical
11016919
AKT1_HUMANAKT1physical
16362038
SMAD4_HUMANSMAD4physical
9311995
NFYC_HUMANNFYCphysical
12023901
SMAD4_HUMANSMAD4physical
11274206
INSR_HUMANINSRphysical
9092546
FOXH1_HUMANFOXH1physical
10938097
RUNX1_HUMANRUNX1physical
10531362
RUNX2_HUMANRUNX2physical
10531362
RUNX3_HUMANRUNX3physical
10531362
SNW1_HUMANSNW1physical
11278756
STRAP_HUMANSTRAPphysical
10757800
STRAP_HUMANSTRAPgenetic
10757800
SMAD4_HUMANSMAD4physical
9892009
SMAD3_HUMANSMAD3genetic
9892009
SMAD7_HUMANSMAD7genetic
9892009
CASL_HUMANNEDD9physical
11118211
SMAD4_HUMANSMAD4physical
11114293
SP1_HUMANSP1physical
11114293
SMAD4_HUMANSMAD4physical
11102446
LEF1_HUMANLEF1physical
10890911
SMAD6_HUMANSMAD6physical
9256479
PIN1_HUMANPIN1physical
19122240
UCHL5_HUMANUCHL5physical
16027725
BPTF_HUMANBPTFphysical
18974875
OBF1_HUMANPOU2AF1physical
20211142
NEDD4_HUMANNEDD4physical
15496141
CITE2_HUMANCITED2physical
16619037
WWP1_HUMANWWP1physical
15221015
SMUF1_HUMANSMURF1physical
15221015
SMUF2_HUMANSMURF2physical
15221015
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
GTF2I_HUMANGTF2Iphysical
16055724
GT2D1_HUMANGTF2IRD1physical
16055724
EVI1_HUMANMECOMphysical
15849193
SMAD2_HUMANSMAD2physical
12700238
SMAD3_HUMANSMAD3physical
12700238
SOX9_HUMANSOX9physical
15623506
SKI_HUMANSKIphysical
10575014
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
SMAD7_HUMANSMAD7physical
17438144
SKI_HUMANSKIphysical
14699069
HDAC1_HUMANHDAC1physical
14699069
SMUF2_HUMANSMURF2physical
11158580
SMAD4_HUMANSMAD4physical
10781087
CTNB1_HUMANCTNNB1physical
20571128
SMUF2_HUMANSMURF2physical
19620243
ATF3_HUMANATF3physical
20930144
ESR1_HUMANESR1physical
20207742
SMUF1_HUMANSMURF1physical
20207742
CBP_HUMANCREBBPphysical
16751102
ARI1B_HUMANARID1Bphysical
16751102
SMCA4_HUMANSMARCA4physical
16751102
SMRC2_HUMANSMARCC2physical
16751102
NCOA3_HUMANNCOA3physical
16751102
SMRC1_HUMANSMARCC1physical
16751102
TRI33_HUMANTRIM33physical
16751102
SMAD4_HUMANSMAD4physical
16751102
CHIP_HUMANSTUB1physical
14701756
WWP2_HUMANWWP2physical
21258410
TGFR1_HUMANTGFBR1physical
18511908
USP9X_HUMANUSP9Xphysical
19135894
SMAD4_HUMANSMAD4physical
10085121
SMAD2_HUMANSMAD2physical
10085121
SKIL_HUMANSKILphysical
12426322
NU214_HUMANNUP214physical
12917407
UBP15_HUMANUSP15physical
21947082
ITCH_HUMANITCHphysical
15350225
TGFR1_HUMANTGFBR1physical
15350225
SKI_HUMANSKIphysical
17283070
CBP_HUMANCREBBPphysical
17283070
SMAD4_HUMANSMAD4physical
17283070
RGCC_HUMANRGCCphysical
21990365
ETV4_HUMANETV4physical
21613609
P53_HUMANTP53physical
19580641
NED4L_HUMANNEDD4Lphysical
19917253
SMAD4_HUMANSMAD4physical
19917253
UBP15_HUMANUSP15physical
22344298
HGS_HUMANHGSphysical
11094085
ZFYV9_HUMANZFYVE9physical
11094085
SMAD4_HUMANSMAD4physical
16916642
SMAD4_HUMANSMAD4physical
18729074
SMAD3_HUMANSMAD3physical
18729074
KC1D_HUMANCSNK1Dphysical
18729074
DDX3Y_HUMANDDX3Yphysical
18729074
ERBIN_HUMANERBB2IPphysical
18729074
HSP74_HUMANHSPA4physical
18729074
MAN1_HUMANLEMD3physical
18729074
ZFYV9_HUMANZFYVE9physical
18729074
SKI_HUMANSKIphysical
18729074
SNW1_HUMANSNW1physical
18729074
SMUF2_HUMANSMURF2physical
18729074
SKIL_HUMANSKILphysical
18729074
WWP2_HUMANWWP2physical
18729074
TYY1_HUMANYY1physical
18729074
OPA1_HUMANOPA1physical
18729074
DCAF7_HUMANDCAF7physical
18729074
ADT2_HUMANSLC25A5physical
18729074
ADT3_HUMANSLC25A6physical
18729074
SQOR_HUMANSQRDLphysical
18729074
BUB3_HUMANBUB3physical
18729074
RIN1_HUMANRIN1physical
18729074
KLF5_HUMANKLF5physical
18729074
SMAD5_HUMANSMAD5physical
18729074
SMAD1_HUMANSMAD1physical
18729074
MPCP_HUMANSLC25A3physical
18729074
ITB4_HUMANITGB4physical
18729074
TCPZ_HUMANCCT6Aphysical
18729074
SARG_HUMANC1orf116physical
18729074
DHX8_HUMANDHX8physical
18729074
U2AF2_HUMANU2AF2physical
18729074
SIK3_HUMANSIK3physical
18729074
DNJA2_HUMANDNAJA2physical
18729074
ATD3B_HUMANATAD3Bphysical
18729074
PCID2_HUMANPCID2physical
18729074
WRIP1_HUMANWRNIP1physical
18729074
PSPC1_HUMANPSPC1physical
18729074
DOCK9_HUMANDOCK9physical
18729074
E41L5_HUMANEPB41L5physical
18729074
PYR1_HUMANCADphysical
18729074
DGKA_HUMANDGKAphysical
18729074
FA83G_HUMANFAM83Gphysical
18729074
CPSF7_HUMANCPSF7physical
18729074
SMAD4_HUMANSMAD4physical
15922743
SMAD4_HUMANSMAD4physical
15761153
ERBIN_HUMANERBB2IPphysical
17591701
IKKA_HUMANCHUKphysical
18268325
SMAD4_HUMANSMAD4physical
15350224
PIN1_HUMANPIN1physical
19920136
RNZ2_HUMANELAC2physical
16636667
NOTC4_HUMANNOTCH4physical
16007227
SMAD1_HUMANSMAD1physical
9111321
SMAD2_HUMANSMAD2physical
9111321
SMAD3_HUMANSMAD3physical
9111321
SMAD4_HUMANSMAD4physical
9111321
PSD11_HUMANPSMD11physical
15231748
LAMA5_HUMANLAMA5physical
15231748
ZEB2_HUMANZEB2physical
15231748
RNBP6_HUMANRANBP6physical
15231748
PLIN3_HUMANPLIN3physical
15231748
UBR5_HUMANUBR5physical
15231748
SNAPN_HUMANSNAPINphysical
15231748
CSH1_HUMANCSH1physical
15231748
CSH2_HUMANCSH1physical
15231748
CP11A_HUMANCYP11A1physical
15231748
SAP_HUMANPSAPphysical
15231748
RU17_HUMANSNRNP70physical
15231748
KAP0_HUMANPRKAR1Aphysical
15231748
RARB_HUMANRARBphysical
15231748
SKIL_HUMANSKILphysical
15231748
RXRA_HUMANRXRAphysical
15231748
TGM2_HUMANTGM2physical
15231748
2AAA_HUMANPPP2R1Aphysical
15231748
SORCN_HUMANSRIphysical
15231748
PEX19_HUMANPEX19physical
15231748
PSMD8_HUMANPSMD8physical
15231748
F10A1_HUMANST13physical
15231748
PAPOA_HUMANPAPOLAphysical
15231748
ZNF41_HUMANZNF41physical
15231748
AFAD_HUMANMLLT4physical
15231748
ANTR2_HUMANANTXR2physical
15231748
RS14_HUMANRPS14physical
15231748
RL40_HUMANUBA52physical
15231748
EF1A1_HUMANEEF1A1physical
15231748
ST5_HUMANST5physical
15231748
KHDR1_HUMANKHDRBS1physical
15231748
PAPP1_HUMANPAPPAphysical
15231748
OS9_HUMANOS9physical
15231748
ROCK1_HUMANROCK1physical
15231748
ANK3_HUMANANK3physical
15231748
NCOA6_HUMANNCOA6physical
15231748
IMB1_HUMANKPNB1physical
15231748
PSG9_HUMANPSG9physical
15231748
ZMY11_HUMANZMYND11physical
15231748
WASC4_HUMANKIAA1033physical
15231748
RS27A_HUMANRPS27Aphysical
15231748
RN123_HUMANRNF123physical
15231748
PAXI1_HUMANPAXIP1physical
15231748
TBCD1_HUMANTBC1D1physical
15231748
DOCK8_HUMANDOCK8physical
15231748
P66B_HUMANGATAD2Bphysical
15231748
CBP_HUMANCREBBPphysical
15231748
CSN5_HUMANCOPS5physical
15231748
CUL5_HUMANCUL5physical
15231748
ABTB1_HUMANABTB1physical
15231748
DCNL1_HUMANDCUN1D1physical
15231748
RBM40_HUMANRNPC3physical
15231748
F161B_HUMANFAM161Bphysical
15231748
NED4L_HUMANNEDD4Lphysical
15231748
RANB9_HUMANRANBP9physical
15231748
DNJC7_HUMANDNAJC7physical
15231748
TRI62_HUMANTRIM62physical
15231748
BTBD2_HUMANBTBD2physical
15231748
CV046_HUMANC22orf46physical
15231748
SMUF2_HUMANSMURF2physical
15231748
SMUF1_HUMANSMURF1physical
15231748
DYHC1_HUMANDYNC1H1physical
15231748
BAZ1A_HUMANBAZ1Aphysical
15231748
CISH_HUMANCISHphysical
15231748
BCD1_HUMANZNHIT6physical
15231748
NAGK_HUMANNAGKphysical
15231748
ANC2_HUMANANAPC2physical
15231748
EIF3L_HUMANEIF3Lphysical
15231748
TGFR1_HUMANTGFBR1physical
12543979
SMAD3_HUMANSMAD3physical
12543979
SMAD4_HUMANSMAD4physical
12543979
SH22A_HUMANSH2D2Aphysical
16806069
MAN1_HUMANLEMD3physical
15489854
IRF7_HUMANIRF7physical
14729983
IRF3_HUMANIRF3physical
14729983
TSC2_HUMANTSC2physical
15066998
FHL1_HUMANFHL1physical
19139564
SMAD4_HUMANSMAD4physical
23788427
TRI33_HUMANTRIM33physical
23788427
SMAD3_HUMANSMAD3physical
21988832
SMAD4_HUMANSMAD4physical
21988832
NFM_HUMANNEFMphysical
20195357
AN32E_HUMANANP32Ephysical
20195357
AN32B_HUMANANP32Bphysical
20195357
TBA1B_HUMANTUBA1Bphysical
20195357
PTMS_HUMANPTMSphysical
20195357
SODC_HUMANSOD1physical
20195357
SYT1_HUMANSYT1physical
20195357
ATP5I_HUMANATP5Iphysical
20195357
JUN_HUMANJUNphysical
20195357
HDAC2_HUMANHDAC2physical
20195357
SMAD4_HUMANSMAD4physical
24157709
FOXH1_HUMANFOXH1physical
15750622
CBP_HUMANCREBBPphysical
15750622
LEF1_HUMANLEF1physical
15750622
DOK1_MOUSEDok1physical
11927552
SMAD4_HUMANSMAD4physical
11927552
NFIA_HUMANNFIAphysical
18215124
PARD3_HUMANPARD3physical
12650946
SMAD4_HUMANSMAD4physical
24584437
KAT2B_HUMANKAT2Bphysical
22995475
SMAD4_HUMANSMAD4physical
25514493
SMAD7_HUMANSMAD7physical
26555259
SMAD4_HUMANSMAD4physical
26555259
NED4L_HUMANNEDD4Lphysical
26555259
SMUF2_HUMANSMURF2physical
28881580
SMAD4_HUMANSMAD4physical
28468752
SMUF2_HUMANSMURF2physical
28468752

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMAD2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The DNA binding activities of Smad2 and Smad3 are regulated bycoactivator-mediated acetylation.";
Simonsson M., Kanduri M., Gronroos E., Heldin C.H., Ericsson J.;
J. Biol. Chem. 281:39870-39880(2006).
Cited for: ACETYLATION AT LYS-19, AND MUTAGENESIS OF LYS-19 AND LYS-20.
Phosphorylation
ReferencePubMed
"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-458, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8 AND SER-458, AND MASSSPECTROMETRY.
"Decorin suppresses transforming growth factor-beta-induced expressionof plasminogen activator inhibitor-1 in human mesangial cells througha mechanism that involves Ca2+-dependent phosphorylation of Smad2 atserine-240.";
Abdel-Wahab N., Wicks S.J., Mason R.M., Chantry A.;
Biochem. J. 362:643-649(2002).
Cited for: PHOSPHORYLATION AT SER-240.
"TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required forSmad2-Smad4 complex formation and signaling.";
Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L.,Wrana J.L.;
J. Biol. Chem. 272:27678-27685(1997).
Cited for: PHOSPHORYLATION AT SER-465 AND SER-467 BY TGFBR1.
"The TGF-beta family mediator Smad1 is phosphorylated directly andactivated functionally by the BMP receptor kinase.";
Kretzschmar M., Liu F., Hata A., Doody J., Massague J.;
Genes Dev. 11:984-995(1997).
Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
"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.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, AND MASSSPECTROMETRY.
"Modulation of Smad2-mediated signaling by extracellular signal-regulated kinase.";
Funaba M., Zimmerman C.M., Mathews L.S.;
J. Biol. Chem. 277:41361-41368(2002).
Cited for: PHOSPHORYLATION AT THR-8; THR-220; SER-245; SER-250 AND SER-255.

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