SMAD3

Functionⁱ

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	40	Required for trimerizationBy similarity	1
Siteⁱ	41	Required for interaction with DNA and JUN and for functional cooperation with JUNBy similarity	1
Metal bindingⁱ	64	ZincBy similarity	1
Metal bindingⁱ	109	ZincBy similarity	1
Metal bindingⁱ	121	ZincBy similarity	1
Metal bindingⁱ	126	ZincBy similarity	1

GO - Molecular functionⁱ

bHLH transcription factor binding Source: Ensembl
chromatin DNA binding Source: Ensembl
collagen binding Source: Ensembl
co-SMAD binding Source: Ensembl
DEAD/H-box RNA helicase binding Source: Ensembl
DNA-binding transcription activator activity, RNA polymerase II-specific Source: Ensembl
DNA-binding transcription factor activity Source: UniProtKB
glucocorticoid receptor binding Source: Ensembl
mineralocorticoid receptor binding Source: Ensembl
phosphatase binding Source: Ensembl
primary miRNA binding Source: Ensembl
protein heterodimerization activity Source: Ensembl
protein homodimerization activity Source: Ensembl
protein kinase binding Source: Ensembl
proximal promoter sequence-specific DNA binding Source: UniProtKB
RNA polymerase II activating transcription factor binding Source: Ensembl
RNA polymerase II proximal promoter sequence-specific DNA binding Source: Ensembl
R-SMAD binding Source: Ensembl
transcription coregulator activity Source: Ensembl
transcription factor activity, RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Source: Ensembl
transforming growth factor beta receptor binding Source: Ensembl
ubiquitin binding Source: Ensembl
ubiquitin protein ligase binding Source: Ensembl
zinc ion binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
cell-cell junction organization Source: Ensembl
cell cycle arrest Source: Ensembl
developmental growth Source: Ensembl
embryonic cranial skeleton morphogenesis Source: Ensembl
embryonic foregut morphogenesis Source: Ensembl
embryonic pattern specification Source: Ensembl
endoderm development Source: Ensembl
evasion or tolerance of host defenses by virus Source: Ensembl
extrinsic apoptotic signaling pathway Source: Ensembl
heart looping Source: Ensembl
immune response Source: Ensembl
immune system development Source: Ensembl
in utero embryonic development Source: Ensembl
lens fiber cell differentiation Source: Ensembl
liver development Source: Ensembl
mesoderm formation Source: Ensembl
negative regulation of cell growth Source: Ensembl
negative regulation of cytosolic calcium ion concentration Source: Ensembl
negative regulation of fat cell differentiation Source: Ensembl
negative regulation of inflammatory response Source: Ensembl
negative regulation of mitotic cell cycle Source: Ensembl
negative regulation of osteoblast differentiation Source: Ensembl
negative regulation of osteoblast proliferation Source: Ensembl
negative regulation of transcription by RNA polymerase II Source: Ensembl
negative regulation of wound healing Source: Ensembl
nodal signaling pathway Source: Ensembl
osteoblast development Source: Ensembl
paraxial mesoderm morphogenesis Source: Ensembl
pericardium development Source: Ensembl
positive regulation of chondrocyte differentiation Source: Ensembl
positive regulation of epithelial to mesenchymal transition Source: Ensembl
positive regulation of extracellular matrix assembly Source: Ensembl
positive regulation of nitric oxide biosynthetic process Source: Ensembl
positive regulation of pri-miRNA transcription by RNA polymerase II Source: Ensembl
regulation of binding Source: Ensembl
regulation of epithelial cell proliferation Source: Ensembl
regulation of immune response Source: Ensembl
regulation of striated muscle tissue development Source: Ensembl
regulation of transforming growth factor beta2 production Source: Ensembl
regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
response to hypoxia Source: Ensembl
SMAD protein complex assembly Source: Ensembl
SMAD protein signal transduction Source: Ensembl
somitogenesis Source: Ensembl
T cell activation Source: Ensembl
thyroid gland development Source: Ensembl
transforming growth factor beta receptor signaling pathway Source: UniProtKB
ureteric bud development Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Transcription, Transcription regulation
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-SSC-1181150 Signaling by NODAL R-SSC-1502540 Signaling by Activin R-SSC-2173788 Downregulation of TGF-beta receptor signaling R-SSC-2173789 TGF-beta receptor signaling activates SMADs R-SSC-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity R-SSC-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription R-SSC-5689880 Ub-specific processing proteases R-SSC-8941855 RUNX3 regulates CDKN1A transcription

Reactomeⁱ

R-SSC-1181150 Signaling by NODAL
R-SSC-1502540 Signaling by Activin
R-SSC-2173788 Downregulation of TGF-beta receptor signaling
R-SSC-2173789 TGF-beta receptor signaling activates SMADs
R-SSC-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-SSC-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-SSC-5689880 Ub-specific processing proteases
R-SSC-8941855 RUNX3 regulates CDKN1A transcription

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Mothers against decapentaplegic homolog 3 Short name: MAD homolog 3 Short name: Mad3 Short name: Mothers against DPP homolog 3 Alternative name(s): SMAD family member 3 Short name: SMAD 3 Short name: Smad3
Gene namesⁱ	Name:SMAD3 Synonyms:MADH3
Organismⁱ	Sus scrofa (Pig)
Taxonomic identifierⁱ	9823 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus
Proteomesⁱ	UP000008227 Componentⁱ: Chromosome 1

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedBy similarity
ChainⁱPRO_0000090858	2 – 425	Mothers against decapentaplegic homolog 3Add BLAST		424

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineBy similarity	1
Modified residueⁱ	8	Phosphothreonine; by CDK2 and CDK4By similarity	1
Cross-linkⁱ	33	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	81	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	179	Phosphothreonine; by CDK2, CDK4 and MAPKBy similarity	1
Modified residueⁱ	204	Phosphoserine; by GSK3 and MAPKPROSITE-ProRule annotationBy similarity	1
Modified residueⁱ	208	Phosphoserine; by MAPKPROSITE-ProRule annotationBy similarity	1
Modified residueⁱ	213	Phosphoserine; by CDK2 and CDK4PROSITE-ProRule annotationBy similarity	1
Modified residueⁱ	378	N6-acetyllysineBy similarity	1
Modified residueⁱ	416	PhosphoserinePROSITE-ProRule annotationBy similarity	1
Modified residueⁱ	418	Phosphoserine; by CK1PROSITE-ProRule annotationBy similarity	1
Modified residueⁱ	422	Phosphoserine; by TGFBR1PROSITE-ProRule annotationBy similarity	1
Modified residueⁱ	423	Phosphoserine; by TGFBR1PROSITE-ProRule annotationBy similarity	1
Modified residueⁱ	425	Phosphoserine; by TGFBR1PROSITE-ProRule annotationBy similarity	1

Post-translational modificationⁱ

Phosphorylated on serine and threonine residues. Enhanced phosphorylation in the linker region on Thr-179, Ser-204 and Ser-208 on EGF and TGF-beta treatment. Ser-208 is the main site of MAPK-mediated phosphorylation. CDK-mediated phosphorylation occurs in a cell-cycle dependent manner and inhibits both the transcriptional activity and antiproliferative functions of SMAD3. This phosphorylation is inhibited by flavopiridol. Maximum phosphorylation at the G₁/S junction. Also phosphorylated on serine residues in the C-terminal SXS motif by TGFBR1 and ACVR1. TGFBR1-mediated phosphorylation at these C-terminal sites is required for interaction with SMAD4, nuclear location and transactivational activity, and appears to be a prerequisite for the TGF-beta mediated phosphorylation in the linker region. Dephosphorylated in the C-terminal SXS motif by PPM1A. This dephosphorylation disrupts the interaction with SMAD4, promotes nuclear export and terminates TGF-beta-mediated signaling. Phosphorylation at Ser-418 by CSNK1G2/CK1 promotes ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Phosphorylated by PDPK1 (By similarity).By similarity

Acetylation in the nucleus by EP300 in the MH2 domain regulates positively its transcriptional activity and is enhanced by TGF-beta.By similarity

Poly-ADP-ribosylated by PARP1 and PARP2. ADP-ribosylation negatively regulates SMAD3 transcriptional responses during the course of TGF-beta signaling.By similarity

Ubiquitinated. Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes. Ubiquitinated by RNF111, leading to its degradation: only SMAD3 proteins that are 'in use' are targeted by RNF111, RNF111 playing a key role in activating SMAD3 and regulating its turnover. Undergoes STUB1-mediated ubiquitination and degradation.By similarity

Keywords - PTMⁱ

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	P84024
PeptideAtlas More...PeptideAtlasⁱ	P84024
PRIDEⁱ	P84024

Expressionⁱ

Tissue specificityⁱ

Highly expressed in the brain and ovary. Detected in the pyramidal cells of the hippocampus, granule cells of the dentate gyrus, granular cells of the cerebral cortex and the granulosa cells of the ovary.

Interactionⁱ

Subunit structureⁱ

Monomer; in the absence of TGF-beta. Homooligomer; in the presence of TGF-beta. Heterotrimer; forms a heterotrimer in the presence of TGF-beta consisting of two molecules of C-terminally phosphorylated SMAD2 or SMAD3 and one of SMAD4 to form the transcriptionally active SMAD2/SMAD3-SMAD4 complex. Interacts with TGFBR1. Interacts (via the MH2 domain) with ZFYVE9. Interacts with HDAC1, TGIF and TGIF2, RUNX3, CREBBP, SKOR1, SKOR2, SNON, ATF2, SMURF2 and SNW1. Interacts with DACH1; the interaction inhibits the TGF-beta signaling. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3. Forms a complex with SMAD2 and TRIM33 upon addition of TGF-beta. Found in a complex with SMAD3, RAN and XPO4. Interacts in the complex directly with XPO4. Interacts (via the MH2 domain) with LEMD3; the interaction represses SMAD3 transcriptional activity through preventing the formation of the heteromeric complex with SMAD4 and translocation to the nucleus. Interacts with RBPMS. Interacts (via MH2 domain) with MECOM. Interacts with WWTR1 (via its coiled-coil domain). Interacts (via the linker region) with EP300 (C-terminal); the interaction promotes SMAD3 acetylation and is enhanced by TGF-beta phosphorylation in the C-terminal of SMAD3. This interaction can be blocked by competitive binding of adenovirus oncoprotein E1A to the same C-terminal site on EP300, which then results in partially inhibited SMAD3/SMAD4 transcriptional activity. Interacts with SKI; the interaction represses SMAD3 transcriptional activity. Component of the multimeric complex SMAD3/SMAD4/JUN/FOS which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. Interacts (via an N-terminal domain) with JUN (via its basic DNA binding and leucine zipper domains); this interaction is essential for DNA binding and cooperative transcriptional activity in response to TGF-beta. Interacts with PPM1A; the interaction dephosphorylates SMAD3 in the C-terminal SXS motif leading to disruption of the SMAD2/3-SMAD4 complex, nuclear export and termination of TGF-beta signaling. Interacts (dephosphorylated form via the MH1 and MH2 domains) with RANBP3 (via its C-terminal R domain); the interaction results in the export of dephosphorylated SMAD3 out of the nucleus and termination of the TGF-beta signaling. Interacts with AIP1, PML, TGFB1I1, TTRAP, FOXL2, PRDM16, HGS and WWP1. Interacts with NEDD4L; the interaction requires TGF-beta stimulation. Interacts with MEN1. Interacts (via MH2 domain) with CITED2 (via C-terminus). Interaction with CSNK1G2. Interacts with PDPK1 (via PH domain). Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation. Interacts with USP15. Interacts with PPP5C; the interaction decreases SMAD3 phosphorylation and protein levels. Interacts with LDLRAD4 (via the SMAD interaction motif). Interacts with PMEPA1. Interacts with ZC3H3. Interacts with ZFHX3. Interacts with ZNF451. Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4. Interacts weakly with ZNF8. Interacts (when phosphorylated) with RNF111; RNF111 acts as an enhancer of the transcriptional responses by mediating ubiquitination and degradation of SMAD3 inhibitors. Interacts with STUB1, HSPA1A, HSPA1B, HSP90AA1 and HSP90AB1.By similarity

GO - Molecular functionⁱ

bHLH transcription factor binding Source: Ensembl
co-SMAD binding Source: Ensembl
DEAD/H-box RNA helicase binding Source: Ensembl
glucocorticoid receptor binding Source: Ensembl
mineralocorticoid receptor binding Source: Ensembl
phosphatase binding Source: Ensembl
protein heterodimerization activity Source: Ensembl
protein homodimerization activity Source: Ensembl
protein kinase binding Source: Ensembl
RNA polymerase II activating transcription factor binding Source: Ensembl
R-SMAD binding Source: Ensembl
transforming growth factor beta receptor binding Source: Ensembl
ubiquitin binding Source: Ensembl
ubiquitin protein ligase binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

Molecular INTeraction database More...MINTⁱ	P84024
STRINGⁱ	9823.ENSSSCP00000005327

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P84024
SMRⁱ	P84024
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	10 – 136	MH1PROSITE-ProRule annotationAdd BLAST		127
Domainⁱ	232 – 425	MH2PROSITE-ProRule annotationAdd BLAST		194

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	137 – 231	LinkerAdd BLAST		95
Regionⁱ	271 – 324	Sufficient for interaction with XPO4By similarityAdd BLAST		54

Domainⁱ

The MH1 domain is required for DNA binding (By similarity). Also binds zinc ions which are necessary for the DNA binding.By similarity

The MH2 domain is required for both homomeric and heteromeric interactions and for transcriptional regulation. Sufficient for nuclear import (By similarity).By similarity

The linker region is required for the TGFbeta-mediated transcriptional activity and acts synergistically with the MH2 domain.By similarity

Sequence similaritiesⁱ

Belongs to the dwarfin/SMAD family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3701 Eukaryota ENOG410XQKU LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000153499
HOVERGENⁱ	HBG053353
InParanoidⁱ	P84024
KEGG Orthology (KO) More...KOⁱ	K04500

Family and domain databases

Gene3Dⁱ	2.60.200.10, 1 hit 3.90.520.10, 1 hit
InterProⁱ	View protein in InterPro IPR013790 Dwarfin IPR003619 MAD_homology1_Dwarfin-type IPR013019 MAD_homology_MH1 IPR017855 SMAD-like_dom_sf IPR001132 SMAD_dom_Dwarfin-type IPR008984 SMAD_FHA_dom_sf IPR036578 SMAD_MH1_sf
PANTHERⁱ	PTHR13703 PTHR13703, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03165 MH1, 1 hit PF03166 MH2, 1 hit
SMARTⁱ	View protein in SMART SM00523 DWA, 1 hit SM00524 DWB, 1 hit
SUPFAMⁱ	SSF49879 SSF49879, 1 hit SSF56366 SSF56366, 1 hit
PROSITEⁱ	View protein in PROSITE PS51075 MH1, 1 hit PS51076 MH2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P84024-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSSILPFTPP IVKRLLGWKK GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE 
        60         70         80         90        100
LEKAITTQNV NTKCITIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH 
       110        120        130        140        150
HELRAMELCE FAFNMKKDEV CVNPYHYQRV ETPVLPPVLV PRHTEIPAEF 
       160        170        180        190        200
PPLDDYSHSI PENTNFPAGI EPQSNIPETP PPGYLSEDGE TSDHQMNHSM 
       210        220        230        240        250
DAGSPNLSPN PMSPAHNNLD LQPVTYCEPA FWCSISYYEL NQRVGETFHA 
       260        270        280        290        300
SQPSMTVDGF TDPSNSERFC LGLLSNVNRN AAVELTRRHI GRGVRLYYIG 
       310        320        330        340        350
GEVFAECLSD SAIFVQSPNC NQRYGWHPAT VCKIPPGCNL KIFNNQEFAA 
       360        370        380        390        400
LLAQSVNQGF EAVYQLTRMC TIRMSFVKGW GAEYRRQTVT STPCWIELHL 
       410        420 
NGPLQWLDKV LTQMGSPSIR CSSVS

Length:425

Mass (Da):48,081

Last modified:July 5, 2004 - v1

Checksum:ⁱ46DF5E8B371321AC

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB052738 mRNA Translation: BAB19634.1
NCBI Reference Sequences More...RefSeqⁱ	NP_999302.1, NM_214137.1
UniGeneⁱ	Ssc.15913

Genome annotation databases

Ensemblⁱ	ENSSSCT00000005464; ENSSSCP00000005327; ENSSSCG00000004952
GeneIDⁱ	397260
KEGGⁱ	ssc:397260

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P84024	Mothers against decapentaplegic homolog 3	)	HUMAN		425	UniRef100_P84022
Mothers against decapentaplegic homolog 3		MOUSE		425
Mothers against decapentaplegic homolog 3		RAT		425
Mothers against decapentaplegic homolog		CALJA		613
Mothers against decapentaplegic homolog (Fragment)		PONAB		279
+84

Protein	Similar proteins		Species	Score	Length	Source
P84024	Mothers against decapentaplegic homolog 3	)	HUMAN		425	UniRef90_P84022
Mothers against decapentaplegic homolog 3		MOUSE		425
Mothers against decapentaplegic homolog 3		RAT		425
Mothers against decapentaplegic homolog		CALJA		613
Mothers against decapentaplegic homolog (Fragment)		PONAB		279
+84

Protein	Similar proteins		Species	Score	Length	Source
P84024	Mothers against decapentaplegic homolog 3	)	HUMAN		425	UniRef50_P84022
Mothers against decapentaplegic homolog 3		MOUSE		425
Mothers against decapentaplegic homolog 3		RAT		425
Mothers against decapentaplegic homolog 2		DANRE		468
Mothers against decapentaplegic homolog 2		PONAB		467
+501

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB052738 mRNA Translation: BAB19634.1
RefSeqⁱ	NP_999302.1, NM_214137.1
UniGeneⁱ	Ssc.15913

3D structure databases

ProteinModelPortalⁱ	P84024
SMRⁱ	P84024
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

MINTⁱ	P84024
STRINGⁱ	9823.ENSSSCP00000005327

Proteomic databases

PaxDbⁱ	P84024
PeptideAtlasⁱ	P84024
PRIDEⁱ	P84024

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSSSCT00000005464; ENSSSCP00000005327; ENSSSCG00000004952
GeneIDⁱ	397260
KEGGⁱ	ssc:397260

Organism-specific databases

CTDⁱ	4088

CTDⁱ

4088

Phylogenomic databases

eggNOGⁱ	KOG3701 Eukaryota ENOG410XQKU LUCA
GeneTreeⁱ	ENSGT00940000153499
HOVERGENⁱ	HBG053353
InParanoidⁱ	P84024
KOⁱ	K04500

Enzyme and pathway databases

Reactomeⁱ	R-SSC-1181150 Signaling by NODAL R-SSC-1502540 Signaling by Activin R-SSC-2173788 Downregulation of TGF-beta receptor signaling R-SSC-2173789 TGF-beta receptor signaling activates SMADs R-SSC-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity R-SSC-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription R-SSC-5689880 Ub-specific processing proteases R-SSC-8941855 RUNX3 regulates CDKN1A transcription

Reactomeⁱ

R-SSC-1181150 Signaling by NODAL
R-SSC-1502540 Signaling by Activin
R-SSC-2173788 Downregulation of TGF-beta receptor signaling
R-SSC-2173789 TGF-beta receptor signaling activates SMADs
R-SSC-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-SSC-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-SSC-5689880 Ub-specific processing proteases
R-SSC-8941855 RUNX3 regulates CDKN1A transcription

Family and domain databases

Gene3Dⁱ	2.60.200.10, 1 hit 3.90.520.10, 1 hit
InterProⁱ	View protein in InterPro IPR013790 Dwarfin IPR003619 MAD_homology1_Dwarfin-type IPR013019 MAD_homology_MH1 IPR017855 SMAD-like_dom_sf IPR001132 SMAD_dom_Dwarfin-type IPR008984 SMAD_FHA_dom_sf IPR036578 SMAD_MH1_sf
PANTHERⁱ	PTHR13703 PTHR13703, 1 hit
Pfamⁱ	View protein in Pfam PF03165 MH1, 1 hit PF03166 MH2, 1 hit
SMARTⁱ	View protein in SMART SM00523 DWA, 1 hit SM00524 DWB, 1 hit
SUPFAMⁱ	SSF49879 SSF49879, 1 hit SSF56366 SSF56366, 1 hit
PROSITEⁱ	View protein in PROSITE PS51075 MH1, 1 hit PS51076 MH2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SMAD3_PIG
Accessionⁱ	P84024Primary (citable) accession number: P84024 Secondary accession number(s): O09064 Q9GKR4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
	Last sequence update:	July 5, 2004
	Last modified:	December 5, 2018
	This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - P84024 (SMAD3_PIG)

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Mothers against decapentaplegic homolog 3

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

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