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Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)

 SMAD6_HUMAN             Reviewed;         496 AA.
O43541; A9J6M5; O43654; Q15799; Q7Z7L4; Q96E31; Q9UKZ3;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
22-NOV-2017, entry version 169.
RecName: Full=Mothers against decapentaplegic homolog 6;
Short=MAD homolog 6;
Short=Mothers against DPP homolog 6;
AltName: Full=SMAD family member 6;
Short=SMAD 6;
Short=Smad6;
Short=hSMAD6;
Name=SMAD6; Synonyms=MADH6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
PubMed=8673135; DOI=10.1038/ng0796-347;
Riggins G.J., Thiagalingam S., Rosenblum E., Weinstein C.L.,
Kern S.E., Hamilton S.R., Willson J.K.V., Markowitz S.D.,
Kinzler K.W., Vogelstein B.V.;
"Mad-related genes in the human.";
Nat. Genet. 13:347-349(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH
ACVR1B; BMPR1B; SMAD1 AND TGFBR1, AND MUTAGENESIS OF GLY-471 AND
478-ARG--ARG-496.
TISSUE=T-cell;
PubMed=9436979; DOI=10.1101/gad.12.2.186;
Hata A., Lagna G., Massague J., Hemmati-Brivanlou A.;
"Smad6 inhibits BMP/Smad1 signaling by specifically competing with the
Smad4 tumor suppressor.";
Genes Dev. 12:186-197(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Placenta;
PubMed=9712726; DOI=10.1006/bbrc.1998.9170;
Afrakhte M., Moren A., Jossan S., Itoh S., Sampath K., Westermark B.,
Heldin C.H., Heldin N.E., ten Dijke P.;
"Induction of inhibitory Smad6 and Smad7 mRNA by TGF-beta family
members.";
Biochem. Biophys. Res. Commun. 249:505-511(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
Hagiwara K., Freeman A.H., McMenamin M.G., Bennett W.P., Nagashima M.,
Minter A.R., Yang K., Takenoshita S., Harris C.C.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
TISSUE=Prostatic carcinoma;
Konrad L., Scheiber J.A., Brandt H., Eickelberg O., Hofmann R.;
"Identification of a new SMAD6 variant in human.";
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Uterus;
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).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B).
Hagiwara K., Freeman A.A.H., McMenamin M.G., Bennett W.P., Yang K.,
Takenoshita S., Harris C.C.;
"Determination of the genomic structure of human Smad3, Smad6 and
Smad7 and the cloning of the human Smad3 promoter.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[8]
REVIEW.
PubMed=9759503; DOI=10.1146/annurev.biochem.67.1.753;
Massague J.;
"TGF-beta signal transduction.";
Annu. Rev. Biochem. 67:753-791(1998).
[9]
REVIEW.
PubMed=10647776; DOI=10.1016/S1359-6101(99)00012-X;
Verschueren K., Huylebroeck D.;
"Remarkable versatility of Smad proteins in the nucleus of
transforming growth factor-beta activated cells.";
Cytokine Growth Factor Rev. 10:187-199(1999).
[10]
REVIEW.
PubMed=10708948; DOI=10.1016/S1359-6101(99)00024-6;
Wrana J.L., Attisano L.;
"The Smad pathway.";
Cytokine Growth Factor Rev. 11:5-13(2000).
[11]
REVIEW.
PubMed=10708949; DOI=10.1016/S1359-6101(99)00025-8;
Miyazono K.;
"TGF-beta signaling by Smad proteins.";
Cytokine Growth Factor Rev. 11:15-22(2000).
[12]
INTERACTION WITH HOXC8.
PubMed=10722652; DOI=10.1074/jbc.275.12.8267;
Bai S., Shi X., Yang X., Cao X.;
"Smad6 as a transcriptional corepressor.";
J. Biol. Chem. 275:8267-8270(2000).
[13]
FUNCTION (ISOFORM B).
PubMed=11284962; DOI=10.1046/j.1440-169X.2001.00562.x;
Krishnan P., King M.W., Neff A.W., Sandusky G.E., Bierman K.L.,
Grinnell B., Smith R.C.;
"Human truncated Smad 6 (Smad 6s) inhibits the BMP pathway in Xenopus
laevis.";
Dev. Growth Differ. 43:115-132(2001).
[14]
INTERACTION WITH STAMBP.
PubMed=11483516; DOI=10.1093/emboj/20.15.4132;
Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S.;
"Promoting bone morphogenetic protein signaling through negative
regulation of inhibitory Smads.";
EMBO J. 20:4132-4142(2001).
[15]
INTERACTION WITH RNF111.
PubMed=14657019; DOI=10.1093/emboj/cdg632;
Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A.,
Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.;
"Arkadia amplifies TGF-beta superfamily signaling through degradation
of Smad7.";
EMBO J. 22:6458-6470(2003).
[16]
INTERACTION WITH AXIN1.
PubMed=16601693; DOI=10.1038/sj.emboj.7601057;
Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z.,
Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.;
"Axin is a scaffold protein in TGF-beta signaling that promotes
degradation of Smad7 by Arkadia.";
EMBO J. 25:1646-1658(2006).
[17]
FUNCTION, AND INTERACTION WITH PELI1.
PubMed=16951688; DOI=10.1038/ni1383;
Choi K.C., Lee Y.S., Lim S., Choi H.K., Lee C.H., Lee E.K., Hong S.,
Kim I.H., Kim S.J., Park S.H.;
"Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor
signaling through direct interaction with the adaptor Pellino-1.";
Nat. Immunol. 7:1057-1065(2006).
[18]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKX, MUTAGENESIS OF
SER-435, AND PHOSPHORYLATION AT SER-435.
PubMed=16491121; DOI=10.1038/sj.onc.1209436;
Glesne D., Huberman E.;
"Smad6 is a protein kinase X phosphorylation substrate and is required
for HL-60 cell differentiation.";
Oncogene 25:4086-4098(2006).
[19]
INVOLVEMENT IN CONGENITAL CARDIOVASCULAR MALFORMATIONS, VARIANT
THR-325, VARIANTS AOVD2 LEU-415 AND PHE-484, AND CHARACTERIZATION OF
VARIANTS AOVD2 LEU-415 AND PHE-484.
PubMed=22275001; DOI=10.1002/humu.22030;
Tan H.L., Glen E., Topf A., Hall D., O'Sullivan J.J., Sneddon L.,
Wren C., Avery P., Lewis R.J., ten Dijke P., Arthur H.M.,
Goodship J.A., Keavney B.D.;
"Nonsynonymous variants in the SMAD6 gene predispose to congenital
cardiovascular malformation.";
Hum. Mutat. 33:720-727(2012).
[20]
UBIQUITINATION AT LYS-173, AND MUTAGENESIS OF LYS-173.
PubMed=23455153; DOI=10.1038/emboj.2013.38;
Zhang X., Zhang J., Bauer A., Zhang L., Selinger D.W., Lu C.X.,
Ten Dijke P.;
"Fine-tuning BMP7 signalling in adipogenesis by UBE2O/E2-230K-mediated
monoubiquitination of SMAD6.";
EMBO J. 32:996-1007(2013).
[21]
INVOLVEMENT IN CRS7, AND VARIANTS CRS7 223-GLN--ARG-496 DEL; LYS-287;
ALA-306; LEU-323; 374-GLU--ARG-496 DEL; CYS-390; 407-GLU--ARG-496 DEL;
CYS-465 AND THR-490.
PubMed=27606499; DOI=10.7554/eLife.20125;
Timberlake A.T., Choi J., Zaidi S., Lu Q., Nelson-Williams C.,
Brooks E.D., Bilguvar K., Tikhonova I., Mane S., Yang J.F.,
Sawh-Martinez R., Persing S., Zellner E.G., Loring E., Chuang C.,
Galm A., Hashim P.W., Steinbacher D.M., DiLuna M.L., Duncan C.C.,
Pelphrey K.A., Zhao H., Persing J.A., Lifton R.P.;
"Two locus inheritance of non-syndromic midline craniosynostosis via
rare SMAD6 and common BMP2 alleles.";
Elife 5:0-0(2016).
-!- FUNCTION: Acts as a mediator of TGF-beta and BMP antiflammatory
activity. Suppresses IL1R-TLR signaling through its direct
interaction with PEL1, preventing NF-kappa-B activation, nuclear
transport and NF-kappa-B-mediated expression of proinflammatory
genes. May block the BMP-SMAD1 signaling pathway by competing with
SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory
elements in target promoter regions. {ECO:0000269|PubMed:16491121,
ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:9436979}.
-!- SUBUNIT: Interacts with NEDD4L (By similarity). Interacts with
WWP1 (By similarity). Interacts with STAMBP and PRKX. Interacts
with RNF111 and AXIN1. Interacts with TGF-beta type I receptor
superfamily members, including ACVR1B, BMPR1B and TGFBR1. In
response to BMP2, but not to TGFB treatment, interacts with SMAD1,
but not with SMAD2, nor with SMAD4; this interaction may inhibit
SMAD1 binding to SMAD4. Interacts with HOXC8 and HOXC9. Interacts
with PELI1; this interaction interferes with PELI1 complex
formation with TRAF6, IRAK1, IRAK4 and MYD88 in response to IL1B
and hence negatively regulates IL1R-TLR signaling. {ECO:0000250,
ECO:0000269|PubMed:10722652, ECO:0000269|PubMed:11483516,
ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16491121,
ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:16951688,
ECO:0000269|PubMed:9436979}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-976374, EBI-976374;
P51817:PRKX; NbExp=5; IntAct=EBI-976374, EBI-4302903;
Q13950:RUNX2; NbExp=3; IntAct=EBI-976374, EBI-976402;
Q15797:SMAD1; NbExp=4; IntAct=EBI-976374, EBI-1567153;
O95630:STAMBP; NbExp=2; IntAct=EBI-4324970, EBI-396676;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16491121}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A;
IsoId=O43541-1; Sequence=Displayed;
Name=B; Synonyms=Smad 6S;
IsoId=O43541-2; Sequence=VSP_006179, VSP_006180;
Name=D;
IsoId=O43541-4; Sequence=VSP_035489, VSP_035490;
-!- TISSUE SPECIFICITY: Ubiquitous in various organs, with higher
levels in lung. Isoform B is up-regulated in diseased heart
tissue.
-!- PTM: Phosphorylated by BMP type 1 receptor kinase and by PRKX.
{ECO:0000269|PubMed:16491121}.
-!- PTM: Monoubiquitinated at Lys-173 by the E2/E3 hybrid ubiquitin-
protein ligase UBE2O, leading to reduced binding affinity for the
activated BMP type I receptor ACVR1/ALK2, thereby enhancing BMP7
and regulating adipocyte differentiation (PubMed:23455153).
Ubiquitinated by WWP1 (By similarity). Ubiquitinated by RNF165,
promoting proteasomal degradation, leading to enhance the BMP-Smad
signaling (By similarity). {ECO:0000250|UniProtKB:O35182,
ECO:0000269|PubMed:23455153}.
-!- PTM: Arginine methylation by PRMT1, which is recruited by BMPR2,
initiates BMP-Induced signaling and induces dissociation from the
BMPR1B receptor at the cell surface leading to derepress
downstream Smad1/Smad5 signaling. {ECO:0000250|UniProtKB:O35182}.
-!- DISEASE: Aortic valve disease 2 (AOVD2) [MIM:614823]: A common
defect in the aortic valve in which two rather than three leaflets
are present. It is often associated with aortic valve
calcification, stenosis and insufficiency. In extreme cases, the
blood flow may be so restricted that the left ventricle fails to
grow, resulting in hypoplastic left heart syndrome.
{ECO:0000269|PubMed:22275001}. Note=The disease is caused by
mutations affecting the gene represented in this entry. SMAD6
variants may contribute to increased risk of congenital
cardiovascular malformations (CVM). CVM is a major cause of
mortality and morbidity in childhood. In most sporadic cases that
cannot be attributed to particular malformation syndromes or
teratogenic exposures, there remains a substantial excess familial
risk, indicating a significant genetic contribution to disease
susceptibility (PubMed:22275001). {ECO:0000269|PubMed:22275001}.
-!- DISEASE: Craniosynostosis 7 (CRS7) [MIM:617439]: A form of
craniosynostosis, a primary abnormality of skull growth involving
premature fusion of one or more cranial sutures. The growth
velocity of the skull often cannot match that of the developing
brain resulting in an abnormal head shape and, in some cases,
increased intracranial pressure, which must be treated promptly to
avoid permanent neurodevelopmental disability.
{ECO:0000269|PubMed:27606499}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Rare heterozygous SMAD6 variants are strongly associated
with non-syndromic midline craniosynostosis and confer a very high
risk for disease development, in the presence of a common risk
allele (rs1884302) near the BMP2 locus.
{ECO:0000269|PubMed:27606499}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; U59914; AAC50792.1; -; mRNA.
EMBL; AF035528; AAB94137.1; -; mRNA.
EMBL; AF043640; AAC00497.1; -; mRNA.
EMBL; AF037469; AAC82331.1; -; mRNA.
EMBL; AF041065; AAF14343.1; -; Genomic_DNA.
EMBL; AF041062; AAF14343.1; JOINED; Genomic_DNA.
EMBL; AF041063; AAF14343.1; JOINED; Genomic_DNA.
EMBL; AF041064; AAF14343.1; JOINED; Genomic_DNA.
EMBL; AM909653; CAP20377.1; -; mRNA.
EMBL; BC012986; AAH12986.1; -; mRNA.
EMBL; AF101474; AAF06841.1; -; Genomic_DNA.
CCDS; CCDS10221.1; -. [O43541-1]
RefSeq; NP_005576.3; NM_005585.4. [O43541-1]
RefSeq; XP_011519863.1; XM_011521561.2. [O43541-2]
UniGene; Hs.153863; -.
ProteinModelPortal; O43541; -.
SMR; O43541; -.
BioGrid; 110266; 47.
CORUM; O43541; -.
DIP; DIP-36708N; -.
IntAct; O43541; 12.
MINT; MINT-1198639; -.
STRING; 9606.ENSP00000288840; -.
iPTMnet; O43541; -.
PhosphoSitePlus; O43541; -.
BioMuta; SMAD6; -.
EPD; O43541; -.
MaxQB; O43541; -.
PaxDb; O43541; -.
PeptideAtlas; O43541; -.
PRIDE; O43541; -.
Ensembl; ENST00000288840; ENSP00000288840; ENSG00000137834. [O43541-1]
Ensembl; ENST00000557916; ENSP00000452955; ENSG00000137834. [O43541-4]
GeneID; 4091; -.
KEGG; hsa:4091; -.
UCSC; uc002aqf.4; human. [O43541-1]
CTD; 4091; -.
DisGeNET; 4091; -.
EuPathDB; HostDB:ENSG00000137834.14; -.
GeneCards; SMAD6; -.
H-InvDB; HIX0132566; -.
HGNC; HGNC:6772; SMAD6.
HPA; HPA061917; -.
MalaCards; SMAD6; -.
MIM; 602931; gene.
MIM; 614823; phenotype.
MIM; 617439; phenotype.
neXtProt; NX_O43541; -.
OpenTargets; ENSG00000137834; -.
Orphanet; 402075; Familial bicuspid aortic valve.
PharmGKB; PA30529; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOVERGEN; HBG053021; -.
InParanoid; O43541; -.
KO; K04677; -.
OMA; CRTVTCC; -.
OrthoDB; EOG091G0XBN; -.
PhylomeDB; O43541; -.
TreeFam; TF314923; -.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-8941326; RUNX2 regulates bone development.
SignaLink; O43541; -.
SIGNOR; O43541; -.
ChiTaRS; SMAD6; human.
GeneWiki; Mothers_against_decapentaplegic_homolog_6; -.
GenomeRNAi; 4091; -.
PRO; PR:O43541; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000137834; -.
CleanEx; HS_SMAD6; -.
ExpressionAtlas; O43541; baseline and differential.
Genevisible; O43541; HS.
GO; GO:0005737; C:cytoplasm; TAS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0070410; F:co-SMAD binding; IPI:BHF-UCL.
GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0030617; F:transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity; IDA:BHF-UCL.
GO; GO:0070698; F:type I activin receptor binding; IDA:BHF-UCL.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0035904; P:aorta development; IEA:Ensembl.
GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; IDA:UniProtKB.
GO; GO:0006955; P:immune response; IMP:BHF-UCL.
GO; GO:0003183; P:mitral valve morphogenesis; ISS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0030279; P:negative regulation of ossification; ISS:BHF-UCL.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0010991; P:negative regulation of SMAD protein complex assembly; IDA:BHF-UCL.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0003184; P:pulmonary valve morphogenesis; ISS:BHF-UCL.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0034616; P:response to laminar fluid shear stress; IEP:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:InterPro.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; IMP:BHF-UCL.
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;
Alternative splicing; Complete proteome; Craniosynostosis;
Disease mutation; DNA-binding; Isopeptide bond; Metal-binding;
Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc.
CHAIN 1 496 Mothers against decapentaplegic homolog
6.
/FTId=PRO_0000090869.
DOMAIN 148 275 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 331 496 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
COMPBIAS 25 33 Poly-Gly.
COMPBIAS 82 85 Poly-Arg.
COMPBIAS 165 168 Poly-Leu.
COMPBIAS 251 254 Poly-Ala.
COMPBIAS 275 278 Poly-Pro.
METAL 205 205 Zinc. {ECO:0000250}.
METAL 247 247 Zinc. {ECO:0000250}.
METAL 260 260 Zinc. {ECO:0000250}.
METAL 265 265 Zinc. {ECO:0000250}.
MOD_RES 75 75 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:O35182}.
MOD_RES 75 75 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:O35182}.
MOD_RES 82 82 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:O35182}.
MOD_RES 82 82 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:O35182}.
MOD_RES 435 435 Phosphoserine; by PRKX; in vitro.
{ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:16491121}.
CROSSLNK 173 173 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:23455153}.
VAR_SEQ 1 261 Missing (in isoform B).
{ECO:0000303|PubMed:8673135}.
/FTId=VSP_006179.
VAR_SEQ 262 273 NPYHFSRLCGPE -> MSRMGKPIETQK (in isoform
B). {ECO:0000303|PubMed:8673135}.
/FTId=VSP_006180.
VAR_SEQ 318 338 DASMSPDATKPSHWCSVAYWE -> AADAGIGSRGNRGLES
SVPCS (in isoform D).
{ECO:0000303|Ref.5}.
/FTId=VSP_035489.
VAR_SEQ 339 496 Missing (in isoform D).
{ECO:0000303|Ref.5}.
/FTId=VSP_035490.
VARIANT 223 496 Missing (in CRS7; associated with disease
susceptibility).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_078924.
VARIANT 287 287 E -> K (in CRS7; associated with disease
susceptibility; dbSNP:rs570279865).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_078925.
VARIANT 306 306 T -> A (in CRS7; associated with disease
susceptibility).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_077592.
VARIANT 323 323 P -> L (in CRS7; associated with disease
susceptibility).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_077593.
VARIANT 325 325 A -> T (found in a patient with
congenital mitral valve prolapse;
dbSNP:rs199822239).
{ECO:0000269|PubMed:22275001}.
/FTId=VAR_068074.
VARIANT 374 496 Missing (in CRS7; associated with disease
susceptibility).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_078926.
VARIANT 390 390 G -> C (in CRS7; associated with disease
susceptibility; de novo mutation).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_077594.
VARIANT 407 496 Missing (in CRS7; associated with disease
susceptibility).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_078927.
VARIANT 415 415 P -> L (in AOVD2; results in
significantly lower activity than wild-
type in inhibiting BMP signaling in a
transcriptional reporter assay;
dbSNP:rs387907284).
{ECO:0000269|PubMed:22275001}.
/FTId=VAR_068075.
VARIANT 465 465 R -> C (in CRS7; associated with disease
susceptibility; dbSNP:rs761888345).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_077595.
VARIANT 484 484 C -> F (in AOVD2; results in
significantly lower activity than wild-
type in inhibiting BMP signaling in a
transcriptional reporter assay;
dbSNP:rs387907283).
{ECO:0000269|PubMed:22275001}.
/FTId=VAR_068076.
VARIANT 490 490 I -> T (in CRS7; associated with disease
susceptibility).
{ECO:0000269|PubMed:27606499}.
/FTId=VAR_078928.
MUTAGEN 173 173 K->R: Abolishes monoubiquitination by
UBE2O. {ECO:0000269|PubMed:23455153}.
MUTAGEN 435 435 S->A: Loss of in vitro phosphorylation by
PRKX. {ECO:0000269|PubMed:16491121}.
MUTAGEN 471 471 G->S: Loss of SMAD1-binding and of
inhibition of BMP-SMAD1 signaling. No
effect on interaction with BMPR1B and
TGFBR1. {ECO:0000269|PubMed:9436979}.
MUTAGEN 478 496 Missing: Loss of interaction with BMPR1B,
TGFBR1 and SMAD1.
{ECO:0000269|PubMed:9436979}.
CONFLICT 21 21 D -> N (in Ref. 2; AAB94137).
{ECO:0000305}.
SEQUENCE 496 AA; 53497 MW; A4B928AE2D34EBC2 CRC64;
MFRSKRSGLV RRLWRSRVVP DREEGGSGGG GGGDEDGSLG SRAEPAPRAR EGGGCGRSEV
RPVAPRRPRD AVGQRGAQGA GRRRRAGGPP RPMSEPGAGA GSSLLDVAEP GGPGWLPESD
CETVTCCLFS ERDAAGAPRD ASDPLAGAAL EPAGGGRSRE ARSRLLLLEQ ELKTVTYSLL
KRLKERSLDT LLEAVESRGG VPGGCVLVPR ADLRLGGQPA PPQLLLGRLF RWPDLQHAVE
LKPLCGCHSF AAAADGPTVC CNPYHFSRLC GPESPPPPYS RLSPRDEYKP LDLSDSTLSY
TETEATNSLI TAPGEFSDAS MSPDATKPSH WCSVAYWEHR TRVGRLYAVY DQAVSIFYDL
PQGSGFCLGQ LNLEQRSESV RRTRSKIGFG ILLSKEPDGV WAYNRGEHPI FVNSPTLDAP
GGRALVVRKV PPGYSIKVFD FERSGLQHAP EPDAADGPYD PNSVRISFAK GWGPCYSRQF
ITSCPCWLEI LLNNPR


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