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Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)

 SMAD3_RAT               Reviewed;         425 AA.
P84025; O09064; O09144; O14510; O35273; Q92940; Q93002; Q9GKR4;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 136.
RecName: Full=Mothers against decapentaplegic homolog 3;
Short=MAD homolog 3;
Short=Mad3;
Short=Mothers against DPP homolog 3;
AltName: Full=SMAD family member 3;
Short=SMAD 3;
Short=Smad3;
Name=Smad3; Synonyms=Madh3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=8917532; DOI=10.1073/pnas.93.23.12992;
Chen Y., Lebrun J.-J., Vale W.W.;
"Regulation of transforming growth factor beta- and activin-induced
transcription by mammalian Mad proteins.";
Proc. Natl. Acad. Sci. U.S.A. 93:12992-12997(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INTERACTION WITH MEN1.
PubMed=11274402; DOI=10.1073/pnas.061358098;
Kaji H., Canaff L., Lebrun J.J., Goltzman D., Hendy G.N.;
"Inactivation of menin, a Smad3-interacting protein, blocks
transforming growth factor type beta signaling.";
Proc. Natl. Acad. Sci. U.S.A. 98:3837-3842(2001).
[4]
INTERACTION WITH CITED2.
PubMed=16619037; DOI=10.1038/sj.onc.1209552;
Chou Y.T., Wang H., Chen Y., Danielpour D., Yang Y.C.;
"Cited2 modulates TGF-beta-mediated upregulation of MMP9.";
Oncogene 25:5547-5560(2006).
-!- FUNCTION: 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). {ECO:0000250|UniProtKB:P84022,
ECO:0000269|PubMed:8917532}.
-!- SUBUNIT: 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. Interaction with CSNK1G2. Interacts (via the MH2 domain)
with ZFYVE9. Interacts with HDAC1, VDR, 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). 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 (By similarity). Interacts with ZFHX3 (By
similarity). Interacts with ZNF451. Identified in a complex that
contains at least ZNF451, SMAD2, SMAD3 and SMAD4 (By similarity).
Interacts weakly with ZNF8. Interacts with STUB1, HSPA1A, HSPA1B,
HSP90AA1 and HSP90AB1 (By similarity).
{ECO:0000250|UniProtKB:P84022, ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000269|PubMed:11274402, ECO:0000269|PubMed:16619037}.
-!- INTERACTION:
P47196:Akt1; NbExp=4; IntAct=EBI-7201857, EBI-7204362;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P84022}.
Nucleus {ECO:0000269|PubMed:8917532}. Note=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 of the nucleus by interaction with RANBP1. Co-
localizes with LEMD3 at the nucleus inner membrane. MAPK-mediated
phosphorylation appears to have no effect on nuclear import. PDPK1
prevents its nuclear translocation in response to TGF-beta.
{ECO:0000250|UniProtKB:P84022}.
-!- TISSUE SPECIFICITY: 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.
-!- DOMAIN: The MH1 domain is required for DNA binding (By
similarity). Also binds zinc ions which are necessary for the DNA
binding. {ECO:0000250}.
-!- DOMAIN: The MH2 domain is required for both homomeric and
heteromeric interactions and for transcriptional regulation.
Sufficient for nuclear import (By similarity). {ECO:0000250}.
-!- DOMAIN: The linker region is required for the TGFbeta-mediated
transcriptional activity and acts synergistically with the MH2
domain. {ECO:0000250}.
-!- PTM: 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 G(1)/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). {ECO:0000250|UniProtKB:P84022}.
-!- PTM: Acetylation in the nucleus by EP300 in the MH2 domain
regulates positively its transcriptional activity and is enhanced
by TGF-beta. {ECO:0000250|UniProtKB:P84022}.
-!- PTM: 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.
{ECO:0000250|UniProtKB:P84022, ECO:0000250|UniProtKB:Q8BUN5}.
-!- PTM: Poly-ADP-ribosylated by PARP1 and PARP2. ADP-ribosylation
negatively regulates SMAD3 transcriptional responses during the
course of TGF-beta signaling. {ECO:0000250|UniProtKB:P84022}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; U66479; AAC52944.1; -; mRNA.
EMBL; BC064437; AAH64437.1; -; mRNA.
RefSeq; NP_037227.1; NM_013095.3.
UniGene; Rn.10636; -.
ProteinModelPortal; P84025; -.
SMR; P84025; -.
BioGrid; 247660; 3.
CORUM; P84025; -.
IntAct; P84025; 1.
MINT; MINT-2739536; -.
STRING; 10116.ENSRNOP00000037346; -.
iPTMnet; P84025; -.
PhosphoSitePlus; P84025; -.
PaxDb; P84025; -.
PRIDE; P84025; -.
Ensembl; ENSRNOT00000039730; ENSRNOP00000037346; ENSRNOG00000008620.
GeneID; 25631; -.
KEGG; rno:25631; -.
UCSC; RGD:3032; rat.
CTD; 4088; -.
RGD; 3032; Smad3.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOVERGEN; HBG053353; -.
InParanoid; P84025; -.
KO; K04500; -.
OMA; SDHQMTH; -.
OrthoDB; EOG091G082C; -.
PhylomeDB; P84025; -.
TreeFam; TF314923; -.
Reactome; R-RNO-1181150; Signaling by NODAL.
Reactome; R-RNO-1502540; Signaling by Activin.
Reactome; R-RNO-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-RNO-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-RNO-5689880; Ub-specific processing proteases.
Reactome; R-RNO-8941855; RUNX3 regulates CDKN1A transcription.
PRO; PR:P84025; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000008620; -.
Genevisible; P84025; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; ISO:RGD.
GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0043235; C:receptor complex; ISO:RGD.
GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
GO; GO:0071144; C:SMAD2-SMAD3 protein complex; ISO:RGD.
GO; GO:0005667; C:transcription factor complex; IDA:RGD.
GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD.
GO; GO:0003682; F:chromatin binding; ISO:RGD.
GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
GO; GO:0070410; F:co-SMAD binding; ISO:RGD.
GO; GO:0005518; F:collagen binding; ISO:RGD.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0035259; F:glucocorticoid receptor binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0031962; F:mineralocorticoid receptor binding; ISO:RGD.
GO; GO:0019902; F:phosphatase binding; ISO:RGD.
GO; GO:0070878; F:primary miRNA binding; ISO:RGD.
GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:RGD.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:RGD.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0046332; F:SMAD binding; IPI:RGD.
GO; GO:0000988; F:transcription factor activity, protein binding; IEA:Ensembl.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; ISO:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:RGD.
GO; GO:0008134; F:transcription factor binding; IDA:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:RGD.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:RGD.
GO; GO:0030618; F:transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; ISO:RGD.
GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:RGD.
GO; GO:0032924; P:activin receptor signaling pathway; ISO:RGD.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0007050; P:cell cycle arrest; ISO:RGD.
GO; GO:0045216; P:cell-cell junction organization; ISO:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
GO; GO:0048589; P:developmental growth; ISO:RGD.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
GO; GO:0048617; P:embryonic foregut morphogenesis; ISO:RGD.
GO; GO:0009880; P:embryonic pattern specification; ISO:RGD.
GO; GO:0007492; P:endoderm development; ISO:RGD.
GO; GO:0019049; P:evasion or tolerance of host defenses by virus; ISO:RGD.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0007369; P:gastrulation; ISO:RGD.
GO; GO:0001947; P:heart looping; ISO:RGD.
GO; GO:0006955; P:immune response; ISO:RGD.
GO; GO:0002520; P:immune system development; ISO:RGD.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0070306; P:lens fiber cell differentiation; ISO:RGD.
GO; GO:0001889; P:liver development; ISO:RGD.
GO; GO:0001707; P:mesoderm formation; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IGI:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:RGD.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
GO; GO:0061767; P:negative regulation of lung blood pressure; IGI:BHF-UCL.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:RGD.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISO:RGD.
GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0061045; P:negative regulation of wound healing; ISO:RGD.
GO; GO:0038092; P:nodal signaling pathway; ISO:RGD.
GO; GO:0002076; P:osteoblast development; ISO:RGD.
GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
GO; GO:0048340; P:paraxial mesoderm morphogenesis; ISO:RGD.
GO; GO:0060039; P:pericardium development; ISO:RGD.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IDA:RGD.
GO; GO:0030501; P:positive regulation of bone mineralization; IDA:RGD.
GO; GO:0035413; P:positive regulation of catenin import into nucleus; IMP:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISO:RGD.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
GO; GO:1901203; P:positive regulation of extracellular matrix assembly; ISO:RGD.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IGI:BHF-UCL.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:RGD.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:RGD.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0032916; P:positive regulation of transforming growth factor beta3 production; IMP:RGD.
GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
GO; GO:0051098; P:regulation of binding; ISO:RGD.
GO; GO:0050678; P:regulation of epithelial cell proliferation; ISO:RGD.
GO; GO:0050776; P:regulation of immune response; ISO:RGD.
GO; GO:0016202; P:regulation of striated muscle tissue development; ISO:RGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISO:RGD.
GO; GO:0001666; P:response to hypoxia; ISO:RGD.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:BHF-UCL.
GO; GO:0001501; P:skeletal system development; ISO:RGD.
GO; GO:0007183; P:SMAD protein complex assembly; IPI:RGD.
GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
GO; GO:0001756; P:somitogenesis; ISO:RGD.
GO; GO:0042110; P:T cell activation; ISO:RGD.
GO; GO:0030878; P:thyroid gland development; ISO:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060290; P:transdifferentiation; IDA:RGD.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0006810; P:transport; ISO:RGD.
GO; GO:0001657; P:ureteric bud development; ISO:RGD.
Gene3D; 2.60.200.10; -; 1.
Gene3D; 3.90.520.10; -; 1.
InterPro; IPR013790; Dwarfin.
InterPro; IPR003619; MAD_homology1_Dwarfin-type.
InterPro; IPR013019; MAD_homology_MH1.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036578; SMAD_MH1_sf.
PANTHER; PTHR13703; PTHR13703; 1.
Pfam; PF03165; MH1; 1.
Pfam; PF03166; MH2; 1.
SMART; SM00523; DWA; 1.
SMART; SM00524; DWB; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56366; SSF56366; 1.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
Acetylation; ADP-ribosylation; Complete proteome; Cytoplasm;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P84022}.
CHAIN 2 425 Mothers against decapentaplegic homolog
3.
/FTId=PRO_0000090859.
DOMAIN 10 136 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 232 425 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
REGION 137 231 Linker.
REGION 271 324 Sufficient for interaction with XPO4.
{ECO:0000250}.
METAL 64 64 Zinc. {ECO:0000250}.
METAL 109 109 Zinc. {ECO:0000250}.
METAL 121 121 Zinc. {ECO:0000250}.
METAL 126 126 Zinc. {ECO:0000250}.
SITE 40 40 Required for trimerization.
{ECO:0000250}.
SITE 41 41 Required for interaction with DNA and JUN
and for functional cooperation with JUN.
{ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P84022}.
MOD_RES 8 8 Phosphothreonine; by CDK2 and CDK4.
{ECO:0000250|UniProtKB:P84022}.
MOD_RES 179 179 Phosphothreonine; by CDK2, CDK4 and MAPK.
{ECO:0000250|UniProtKB:P84022}.
MOD_RES 204 204 Phosphoserine; by GSK3 and MAPK.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 208 208 Phosphoserine; by MAPK.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 213 213 Phosphoserine; by CDK2 and CDK4.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 378 378 N6-acetyllysine.
{ECO:0000250|UniProtKB:P84022}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 418 418 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 422 422 Phosphoserine; by TGFBR1.
{ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 423 423 Phosphoserine; by TGFBR1.
{ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 425 425 Phosphoserine; by TGFBR1.
{ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439}.
SEQUENCE 425 AA; 48081 MW; 46DF5E8B371321AC CRC64;
MSSILPFTPP IVKRLLGWKK GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE LEKAITTQNV
NTKCITIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELRAMELCE FAFNMKKDEV
CVNPYHYQRV ETPVLPPVLV PRHTEIPAEF PPLDDYSHSI PENTNFPAGI EPQSNIPETP
PPGYLSEDGE TSDHQMNHSM DAGSPNLSPN PMSPAHNNLD LQPVTYCEPA FWCSISYYEL
NQRVGETFHA SQPSMTVDGF TDPSNSERFC LGLLSNVNRN AAVELTRRHI GRGVRLYYIG
GEVFAECLSD SAIFVQSPNC NQRYGWHPAT VCKIPPGCNL KIFNNQEFAA LLAQSVNQGF
EAVYQLTRMC TIRMSFVKGW GAEYRRQTVT STPCWIELHL NGPLQWLDKV LTQMGSPSIR
CSSVS


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