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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_PIG               Reviewed;         425 AA.
P84024; O09064; O09144; O14510; O35273; Q92940; Q93002; Q9GKR4;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
02-DEC-2020, entry version 135.
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;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
Yoshiyasu I., Takashi A., Ito Y., Awata T.;
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
-!- 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.
{ECO:0000250|UniProtKB:P84022}.
-!- SUBUNIT: Monomer; in the absence of TGF-beta (By similarity).
Homooligomer; in the presence of TGF-beta (By similarity).
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 (By similarity). Part of a complex consisting
of AIP1, ACVR2A, ACVR1B and SMAD3 (By similarity). Forms a complex with
SMAD2 and TRIM33 upon addition of TGF-beta (By similarity). Found in a
complex composed of SMAD3, RAN and XPO4; within the complex interacts
directly with XPO4 (By similarity). 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 (By
similarity). 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 (By similarity). Identified in a complex that
contains at least ZNF451, SMAD2, SMAD3 and SMAD4 (By similarity).
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 (By similarity).
Interacts (via MH2 domain) with ZMIZ1 (via SP-RING-type domain); in the
TGF-beta signaling pathway increases the activity of the SMAD3/SMAD4
transcriptional complex (By similarity). Interacts (when
phosphorylated) with RNF111; RNF111 acts as an enhancer of the
transcriptional responses by mediating ubiquitination and degradation
of SMAD3 inhibitors (By similarity). 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 (By similarity).
Interacts (via 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 (By
similarity). 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 (By similarity). 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 (By
similarity). Interacts with TGFBR1 (By similarity). Interacts with
TGFB1I1 (By similarity). Interacts with PRDM16 (By similarity).
Interacts with SNW1 (By similarity). Interacts (via MH2 domain) with
ZFYVE9 (By similarity). Interacts with HDAC1 (By similarity). Interacts
with TGIF2 (By similarity). Interacts with SKOR1 (By similarity).
Interacts with SKOR2 (By similarity). Interacts with DACH1; the
interaction inhibits the TGF-beta signaling (By similarity). Interacts
with RBPMS (By similarity). Interacts (via MH2 domain) with MECOM (By
similarity). Interacts with WWTR1 (via its coiled-coil domain) (By
similarity). Interacts with SKI; the interaction represses SMAD3
transcriptional activity (By similarity). Interacts with MEN1 (By
similarity). Interacts with IL1F7 (By similarity). Interaction with
CSNK1G2 (By similarity). Interacts with PDPK1 (via PH domain) (By
similarity). Interacts with DAB2; the interactions are enhanced upon
TGF-beta stimulation (By similarity). Interacts with USP15 (By
similarity). Interacts with PPP5C; the interaction decreases SMAD3
phosphorylation and protein levels (By similarity). Interacts with
LDLRAD4 (via the SMAD interaction motif) (By similarity). Interacts
with PMEPA1 (By similarity). Interacts with ZNF451 (By similarity).
Interacts with ZFHX3 (By similarity). Interacts weakly with ZNF8 (By
similarity). Interacts with STUB1, HSPA1A, HSPA1B, HSP90AA1 and
HSP90AB1 (By similarity). Interacts with YAP1 (when phosphorylated at
'Ser-55') (By similarity). Interacts with AIP1 (By similarity).
Interacts (via MH2 domain) with CITED2 (via C-terminus) (By
similarity). Interacts with HGS (By similarity). Interacts with WWP1
(By similarity). Interacts with TTRAP (By similarity). Interacts with
FOXL2 (By similarity). Interacts with PML (By similarity). Interacts
with NEDD4L; the interaction requires TGF-beta stimulation (By
similarity). Interacts with ZC3H3 (By similarity). Interacts with TGIF.
Interacts with CREBBP. Interacts with ATF2.
{ECO:0000250|UniProtKB:P84022, ECO:0000250|UniProtKB:P84025,
ECO:0000250|UniProtKB:Q8BUN5}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P84022}. Nucleus
{ECO:0000250|UniProtKB:P84022}. Note=Cytoplasmic and nuclear in the
absence of TGF-beta (By similarity). On TGF-beta stimulation, migrates
to the nucleus when complexed with SMAD4 (By similarity). Through the
action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex,
and exported out of the nucleus by interaction with RANBP1 (By
similarity). Co-localizes with LEMD3 at the nucleus inner membrane (By
similarity). MAPK-mediated phosphorylation appears to have no effect on
nuclear import (By similarity). PDPK1 prevents its nuclear
translocation in response to TGF-beta (By similarity). Localized mainly
to the nucleus in the early stages of embryo development with
expression becoming evident in the cytoplasm of the inner cell mass at
the blastocyst stage (By similarity). {ECO:0000250|UniProtKB:P84022,
ECO:0000250|UniProtKB:Q8BUN5}.
-!- 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: 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}.
-!- 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}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AB052738; BAB19634.1; -; mRNA.
RefSeq; NP_999302.1; NM_214137.1.
SMR; P84024; -.
MINT; P84024; -.
STRING; 9823.ENSSSCP00000005327; -.
PaxDb; P84024; -.
PeptideAtlas; P84024; -.
PRIDE; P84024; -.
Ensembl; ENSSSCT00000005464; ENSSSCP00000005327; ENSSSCG00000004952.
Ensembl; ENSSSCT00005057440; ENSSSCP00005035375; ENSSSCG00005035367.
Ensembl; ENSSSCT00015062164; ENSSSCP00015024943; ENSSSCG00015045925.
Ensembl; ENSSSCT00025043673; ENSSSCP00025018565; ENSSSCG00025032064.
Ensembl; ENSSSCT00030064740; ENSSSCP00030029587; ENSSSCG00030046321.
Ensembl; ENSSSCT00035076339; ENSSSCP00035031189; ENSSSCG00035057061.
Ensembl; ENSSSCT00040041424; ENSSSCP00040017352; ENSSSCG00040030551.
Ensembl; ENSSSCT00045018396; ENSSSCP00045012692; ENSSSCG00045010800.
Ensembl; ENSSSCT00050004607; ENSSSCP00050001837; ENSSSCG00050003377.
Ensembl; ENSSSCT00055059976; ENSSSCP00055048056; ENSSSCG00055030102.
Ensembl; ENSSSCT00060092092; ENSSSCP00060039794; ENSSSCG00060067444.
Ensembl; ENSSSCT00070014919; ENSSSCP00070012342; ENSSSCG00070007681.
GeneID; 397260; -.
KEGG; ssc:397260; -.
CTD; 4088; -.
VGNC; VGNC:93217; SMAD3.
eggNOG; KOG3701; Eukaryota.
GeneTree; ENSGT00940000153499; -.
InParanoid; P84024; -.
OMA; NPVSPAH; -.
OrthoDB; 608001at2759; -.
Proteomes; UP000008227; Chromosome 1.
Proteomes; UP000314985; Chromosome 1.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
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.
2: Evidence at transcript level;
Acetylation; ADP-ribosylation; Cytoplasm; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P84022"
CHAIN 2..425
/note="Mothers against decapentaplegic homolog 3"
/id="PRO_0000090858"
DOMAIN 10..136
/note="MH1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
DOMAIN 232..425
/note="MH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
REGION 137..231
/note="Linker"
REGION 271..324
/note="Sufficient for interaction with XPO4"
/evidence="ECO:0000250"
METAL 64
/note="Zinc"
/evidence="ECO:0000250"
METAL 109
/note="Zinc"
/evidence="ECO:0000250"
METAL 121
/note="Zinc"
/evidence="ECO:0000250"
METAL 126
/note="Zinc"
/evidence="ECO:0000250"
SITE 40
/note="Required for trimerization"
/evidence="ECO:0000250"
SITE 41
/note="Required for interaction with DNA and JUN and for
functional cooperation with JUN"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 8
/note="Phosphothreonine; by CDK2 and CDK4"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 179
/note="Phosphothreonine; by CDK2, CDK4 and MAPK"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 204
/note="Phosphoserine; by GSK3 and MAPK"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 208
/note="Phosphoserine; by MAPK"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 213
/note="Phosphoserine; by CDK2 and CDK4"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 378
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 416
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 418
/note="Phosphoserine; by CK1"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 422
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 423
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 425
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439"
CROSSLNK 33
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P84022"
CROSSLNK 81
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P84022"
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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WP980: Wnt Signaling Pathway NetPath
WP1083: Cell cycle
WP258: TGF-beta Receptor Signaling Pathway
WP815: Id Signaling Pathway
WP155: Adipogenesis
WP505: TGF Beta Signaling Pathway
WP179: Cell cycle
WP560: TGF Beta Signaling Pathway
WP1103: Alpha6-Beta4 Integrin Signaling Pathway
WP273: Ovarian Infertility Genes

Related Genes :
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
[SMAD7 MADH7 MADH8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7) (hSMAD7)
[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)
[Smad7 Madh7 Madh8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)
[SMAD2 MADH2 MADR2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2)
[Smad1 Madh1 Madr1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Dwarfin-A) (Dwf-A) (Mothers-against-DPP-related 1) (Mad-related protein 1) (mMad1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD1 BSP1 MADH1 MADR1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[Smad4 Dpc4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[Smad1 Mad1 Madh1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[Smox Dmel\CG2262 DSMAD2 DSmad2 dSMAD2 dSmad2 dsmad2 l(1)G0348 Sad sad Smad SMAD2 Smad2 smad2 SMOX SmoX smox ted tmp CG2262 Dmel_CG2262] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[SMAD4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)
[ZFYVE9 MADHIP SARA SMADIP] Zinc finger FYVE domain-containing protein 9 (Mothers against decapentaplegic homolog-interacting protein) (Madh-interacting protein) (Novel serine protease) (NSP) (Receptor activation anchor) (hSARA) (Smad anchor for receptor activation)
[Mad CG12399] Protein mothers against dpp
[NFKBIA IKBA MAD3 NFKBI] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Major histocompatibility complex enhancer-binding protein MAD3)
[Dper\GL20193 Dper_GL20193] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dsec\GM11208 Dsec_GM11208] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Bcar3] Breast cancer anti-estrogen resistance protein 3 homolog (BCAR3 adapter protein, NSP family member) (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B) (p130Cas-binding protein AND-34)
[Dana\GF20979 dana_GLEANR_4213 Dana_GF20979 GF20979] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Bcar3 And34] Breast cancer anti-estrogen resistance protein 3 homolog (p130Cas-binding protein AND-34)

Bibliography :
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