SMAD3_MOUSE - dbPTM
SMAD3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAD3_MOUSE
UniProt AC Q8BUN5
Protein Name Mothers against decapentaplegic homolog 3
Gene Name Smad3
Organism Mus musculus (Mouse).
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. Through the action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out
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 (By similarity)..
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		26.53-
2Phosphorylation------MSSILPFTP
------CCCCCCCCH		26.5325338131
8PhosphorylationMSSILPFTPPIVKRL
CCCCCCCCHHHHHHH		26.6426824392
37PhosphorylationWCEKAVKSLVKKLKK
HHHHHHHHHHHHHHH		31.62-
78PhosphorylationLDGRLQVSHRKGLPH
CCCCEEEECCCCCCE		12.4725338131
88PhosphorylationKGLPHVIYCRLWRWP
CCCCEEEEEEECCCC		3.1429514104
121S-nitrosocysteineNMKKDEVCVNPYHYQ
HCCCCCEEECCCCCC		2.00-
121S-nitrosylationNMKKDEVCVNPYHYQ
HCCCCCEEECCCCCC		2.0021278135
132PhosphorylationYHYQRVETPVLPPVL
CCCCCCCCCCCCCCC		18.8127180971
179PhosphorylationPQSNIPETPPPGYLS
CCCCCCCCCCCCCCC		35.42-
204PhosphorylationNHSMDAGSPNLSPNP
CCCCCCCCCCCCCCC		16.61-
208PhosphorylationDAGSPNLSPNPMSPA
CCCCCCCCCCCCCCC		29.30-
213PhosphorylationNLSPNPMSPAHNNLD
CCCCCCCCCCCCCCC		21.86-
270S-palmitoylationPSNSERFCLGLLSNV
CCCCHHHHHHHHHCC		3.5428526873
309PhosphorylationEVFAECLSDSAIFVQ
HHHHHHHCCCEEEEE		40.9717991884
324PhosphorylationSPNCNQRYGWHPATV
CCCCCCCCCCCCCCE		18.1429514104
375PhosphorylationRMCTIRMSFVKGWGA
HHHHHHHHHHCCCCC		19.6222871156
378AcetylationTIRMSFVKGWGAEYR
HHHHHHHCCCCCCHH		47.11-
384PhosphorylationVKGWGAEYRRQTVTS
HCCCCCCHHCEECCC		15.5722871156
388PhosphorylationGAEYRRQTVTSTPCW
CCCHHCEECCCCCEE		24.7617991884
391PhosphorylationYRRQTVTSTPCWIEL
HHCEECCCCCEEEEE		26.4722817900
416PhosphorylationKVLTQMGSPSIRCSS
HHHHHCCCCCCCCCC		15.3329514104
418PhosphorylationLTQMGSPSIRCSSVS
HHHCCCCCCCCCCCC		25.10-
422PhosphorylationGSPSIRCSSVS----
CCCCCCCCCCC----		24.759380693
423PhosphorylationSPSIRCSSVS-----
CCCCCCCCCC-----		29.9721982233
425PhosphorylationSIRCSSVS-------
CCCCCCCC-------		36.1321982233
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
8TPhosphorylationKinaseCDK2P97377
Uniprot
8TPhosphorylationKinaseCDK4P30285
Uniprot
179TPhosphorylationKinaseCDK2P97377
Uniprot
179TPhosphorylationKinaseCDK4P30285
Uniprot
179TPhosphorylationKinaseMAPK-Uniprot
204SPhosphorylationKinaseMAPK-Uniprot
204SPhosphorylationKinaseGSK3-Uniprot
208SPhosphorylationKinaseMAPK-Uniprot
213SPhosphorylationKinaseCDK2P97377
Uniprot
213SPhosphorylationKinaseCDK4P30285
Uniprot
309SPhosphorylationKinasePKG1P0C605
PSP
388TPhosphorylationKinasePKG1P0C605
PSP
418SPhosphorylationKinaseCK1-Uniprot
422SPhosphorylationKinaseTGFBR1Q64729
Uniprot
423SPhosphorylationKinaseTGFBR1Q64729
Uniprot
425SPhosphorylationKinaseTGFBR1Q64729
Uniprot
-KUbiquitinationE3 ubiquitin ligaseBtrcQ3ULA2
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseStub1Q9WUD1
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
179TPhosphorylation

-
204SPhosphorylation

-
208SPhosphorylation

-
208SPhosphorylation

-
418SPhosphorylation

-
418Subiquitylation

-
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSK3B_MOUSEGsk3bphysical
18172167
SMAD4_MOUSESmad4physical
17226765
SNAI1_MOUSESnai1physical
19597490
HIF1A_MOUSEHif1aphysical
17053163
MYOD1_MOUSEMyod1physical
20211142
VDR_MOUSEVdrphysical
20211142
AXIN1_MOUSEAxin1physical
16601693
SMAD4_MOUSESmad4physical
22045334
SMAD3_HUMANSMAD3physical
20360068
FETUA_HUMANAHSGphysical
20360068
MAN1_HUMANLEMD3physical
20360068
IKKA_MOUSEChukphysical
18268325
MYOD1_MOUSEMyod1physical
11711431
PEX6_MOUSEPex6physical
14651998
4ET_MOUSEEif4enif1physical
14651998
ZMYM2_MOUSEZmym2physical
14651998
PBX1_MOUSEPbx1physical
14764653
PKNX1_MOUSEPknox1physical
14764653
SMAD4_MOUSESmad4physical
14764653
SMAD4_MOUSESmad4physical
12145309
SMAD4_MOUSESmad4physical
21145499
YAP1_MOUSEYap1physical
21145499
ANXA7_HUMANANXA7physical
26496610
CO5A1_HUMANCOL5A1physical
26496610
IF4B_HUMANEIF4Bphysical
26496610
GDIB_HUMANGDI2physical
26496610
GMDS_HUMANGMDSphysical
26496610
HD_HUMANHTTphysical
26496610
RPB7_HUMANPOLR2Gphysical
26496610
PCP_HUMANPRCPphysical
26496610
RBBP6_HUMANRBBP6physical
26496610
RBM4_HUMANRBM4physical
26496610
ROCK1_HUMANROCK1physical
26496610
STXB2_HUMANSTXBP2physical
26496610
TAF7_HUMANTAF7physical
26496610
TBX3_HUMANTBX3physical
26496610
BAG6_HUMANBAG6physical
26496610
UBL4A_HUMANUBL4Aphysical
26496610
DHX16_HUMANDHX16physical
26496610
FUBP1_HUMANFUBP1physical
26496610
ZFYV9_HUMANZFYVE9physical
26496610
GA2L1_HUMANGAS2L1physical
26496610
WWP1_HUMANWWP1physical
26496610
IQEC2_HUMANIQSEC2physical
26496610
MAN1_HUMANLEMD3physical
26496610
PPIL2_HUMANPPIL2physical
26496610
ASCC1_HUMANASCC1physical
26496610
STX18_HUMANSTX18physical
26496610
GPAM1_HUMANGPALPP1physical
26496610
4ET_HUMANEIF4ENIF1physical
26496610
S39AA_HUMANSLC39A10physical
26496610
DOCK6_HUMANDOCK6physical
26496610
P3H1_HUMANP3H1physical
26496610
TB10A_HUMANTBC1D10Aphysical
26496610
WDR75_HUMANWDR75physical
26496610
IP6K3_HUMANIP6K3physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMAD3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Transforming growth factor beta-induced phosphorylation of Smad3 isrequired for growth inhibition and transcriptional induction inepithelial cells.";
Liu X., Sun Y., Constantinescu S.N., Karam E., Weinberg R.A.,Lodish H.F.;
Proc. Natl. Acad. Sci. U.S.A. 94:10669-10674(1997).
Cited for: PHOSPHORYLATION AT SER-422; SER-423 AND SER-425.

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