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Mothers against decapentaplegic homolog 9 (MAD homolog 9) (Mothers against DPP homolog 9) (Madh6) (SMAD family member 9) (SMAD 9) (Smad9)

 SMAD9_HUMAN             Reviewed;         467 AA.
O15198; A2A2Y6; O14989; Q5TBA1;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
23-MAY-2018, entry version 190.
RecName: Full=Mothers against decapentaplegic homolog 9;
Short=MAD homolog 9;
Short=Mothers against DPP homolog 9;
AltName: Full=Madh6;
AltName: Full=SMAD family member 9;
Short=SMAD 9;
Short=Smad9;
Name=SMAD9;
Synonyms=MADH6, MADH9, SMAD8 {ECO:0000303|PubMed:25755279};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
TISSUE=Fetal brain;
PubMed=9205116; DOI=10.1006/geno.1997.4753;
Watanabe T.K., Suzuki M., Omori Y., Hishigaki H., Horie M.,
Kanemoto N., Fujiwara T., Nakamura Y., Takahashi E.;
"Cloning and characterization of a novel member of the human Mad gene
family (MADH6).";
Genomics 42:446-451(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
TISSUE=Brain, and Eye;
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).
[5]
REVIEW.
PubMed=9759503; DOI=10.1146/annurev.biochem.67.1.753;
Massague J.;
"TGF-beta signal transduction.";
Annu. Rev. Biochem. 67:753-791(1998).
[6]
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).
[7]
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).
[8]
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).
[9]
INTERACTION WITH RANBP3L.
PubMed=25755279; DOI=10.1128/MCB.00121-15;
Chen F., Lin X., Xu P., Zhang Z., Chen Y., Wang C., Han J., Zhao B.,
Xiao M., Feng X.H.;
"Nuclear export of Smads by RanBP3L regulates bone morphogenetic
protein signaling and mesenchymal stem cell differentiation.";
Mol. Cell. Biol. 35:1700-1711(2015).
[10]
VARIANT PPH2 GLU-43, AND CHARACTERIZATION OF VARIANT PPH2 GLU-43.
PubMed=21898662; DOI=10.1002/humu.21605;
Nasim M.T., Ogo T., Ahmed M., Randall R., Chowdhury H.M., Snape K.M.,
Bradshaw T.Y., Southgate L., Lee G.J., Jackson I., Lord G.M.,
Gibbs J.S., Wilkins M.R., Ohta-Ogo K., Nakamura K., Girerd B.,
Coulet F., Soubrier F., Humbert M., Morrell N.W., Trembath R.C.,
Machado R.D.;
"Molecular genetic characterization of SMAD signaling molecules in
pulmonary arterial hypertension.";
Hum. Mutat. 32:1385-1389(2011).
-!- FUNCTION: Transcriptional modulator activated by BMP (bone
morphogenetic proteins) type 1 receptor kinase. SMAD9 is a
receptor-regulated SMAD (R-SMAD).
-!- SUBUNIT: Interaction with the co-SMAD SMAD4. Interacts with PEBP2-
alpha subunit. Interacts with RANBP3L (PubMed:25755279).
{ECO:0000269|PubMed:25755279}.
-!- INTERACTION:
O60341:KDM1A; NbExp=2; IntAct=EBI-748763, EBI-710124;
Q96LA8:PRMT6; NbExp=2; IntAct=EBI-748763, EBI-912440;
Q13485:SMAD4; NbExp=4; IntAct=EBI-12273450, EBI-347263;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=In the cytoplasm in the absence of ligand.
Migration to the nucleus when complexed with SMAD4 (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=O15198-1; Sequence=Displayed;
Name=B;
IsoId=O15198-2; Sequence=VSP_006182;
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
skeletal muscle, prostate, testis, ovary and small intestine. Also
expressed in fetal brain, lung and kidney.
-!- PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins)
type 1 receptor kinase.
-!- DISEASE: Pulmonary hypertension, primary, 2 (PPH2) [MIM:615342]: A
rare disorder characterized by plexiform lesions of proliferating
endothelial cells in pulmonary arterioles. The lesions lead to
elevated pulmonary arterial pression, right ventricular failure,
and death. The disease can occur from infancy throughout life and
it has a mean age at onset of 36 years. Penetrance is reduced.
Although familial pulmonary hypertension is rare, cases secondary
to known etiologies are more common and include those associated
with the appetite-suppressant drugs.
{ECO:0000269|PubMed:21898662}. Note=The disease may be caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D83760; BAA21128.1; -; mRNA.
EMBL; D83761; BAA21129.1; -; mRNA.
EMBL; AL138706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08571.1; -; Genomic_DNA.
EMBL; CH471075; EAX08572.1; -; Genomic_DNA.
EMBL; BC011559; AAH11559.1; -; mRNA.
EMBL; BC104760; AAI04761.1; -; mRNA.
EMBL; BC104762; AAI04763.1; -; mRNA.
EMBL; BC143240; AAI43241.1; -; mRNA.
CCDS; CCDS45032.1; -. [O15198-1]
CCDS; CCDS9360.1; -. [O15198-2]
RefSeq; NP_001120689.1; NM_001127217.2. [O15198-1]
RefSeq; NP_005896.1; NM_005905.5. [O15198-2]
UniGene; Hs.123119; -.
ProteinModelPortal; O15198; -.
SMR; O15198; -.
BioGrid; 110268; 114.
CORUM; O15198; -.
IntAct; O15198; 100.
MINT; O15198; -.
STRING; 9606.ENSP00000369154; -.
iPTMnet; O15198; -.
PhosphoSitePlus; O15198; -.
BioMuta; SMAD9; -.
MaxQB; O15198; -.
PaxDb; O15198; -.
PeptideAtlas; O15198; -.
PRIDE; O15198; -.
DNASU; 4093; -.
Ensembl; ENST00000350148; ENSP00000239885; ENSG00000120693. [O15198-2]
Ensembl; ENST00000379826; ENSP00000369154; ENSG00000120693. [O15198-1]
Ensembl; ENST00000399275; ENSP00000382216; ENSG00000120693. [O15198-1]
GeneID; 4093; -.
KEGG; hsa:4093; -.
UCSC; uc001uvw.3; human. [O15198-1]
CTD; 4093; -.
DisGeNET; 4093; -.
EuPathDB; HostDB:ENSG00000120693.13; -.
GeneCards; SMAD9; -.
HGNC; HGNC:6774; SMAD9.
HPA; CAB009119; -.
HPA; HPA031162; -.
MalaCards; SMAD9; -.
MIM; 603295; gene.
MIM; 615342; phenotype.
neXtProt; NX_O15198; -.
OpenTargets; ENSG00000120693; -.
Orphanet; 275777; Heritable pulmonary arterial hypertension.
PharmGKB; PA30531; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOGENOM; HOG000286018; -.
HOVERGEN; HBG053353; -.
InParanoid; O15198; -.
KO; K16791; -.
OMA; SDFRPVC; -.
OrthoDB; EOG091G082C; -.
PhylomeDB; O15198; -.
TreeFam; TF314923; -.
Reactome; R-HSA-201451; Signaling by BMP.
SIGNOR; O15198; -.
ChiTaRS; SMAD9; human.
GeneWiki; Mothers_against_decapentaplegic_homolog_9; -.
GenomeRNAi; 4093; -.
PRO; PR:O15198; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000120693; -.
CleanEx; HS_SMAD9; -.
ExpressionAtlas; O15198; baseline and differential.
Genevisible; O15198; HS.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005622; C:intracellular; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0071141; C:SMAD protein complex; NAS:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0030618; F:transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; TAS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; ISS:BHF-UCL.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0071773; P:cellular response to BMP stimulus; NAS:BHF-UCL.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0030902; P:hindbrain development; IEA:Ensembl.
GO; GO:0030901; P:midbrain development; IEA:Ensembl.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; TAS:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; ISS: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.
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; Cytoplasm; Disease mutation;
DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation; Zinc.
CHAIN 1 467 Mothers against decapentaplegic homolog
9.
/FTId=PRO_0000090875.
DOMAIN 16 140 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 273 467 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
COMPBIAS 43 49 Poly-Lys.
METAL 68 68 Zinc. {ECO:0000250}.
METAL 113 113 Zinc. {ECO:0000250}.
METAL 125 125 Zinc. {ECO:0000250}.
METAL 130 130 Zinc. {ECO:0000250}.
VAR_SEQ 224 260 Missing (in isoform B).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9205116}.
/FTId=VSP_006182.
VARIANT 43 43 K -> E (in PPH2; affects SMAD-mediated
signaling; dbSNP:rs397514715).
{ECO:0000269|PubMed:21898662}.
/FTId=VAR_066871.
SEQUENCE 467 AA; 52493 MW; CFC8F982945BC6DD CRC64;
MHSTTPISSL FSFTSPAVKR LLGWKQGDEE EKWAEKAVDS LVKKLKKKKG AMDELERALS
CPGQPSKCVT IPRSLDGRLQ VSHRKGLPHV IYCRVWRWPD LQSHHELKPL ECCEFPFGSK
QKEVCINPYH YRRVETPVLP PVLVPRHSEY NPQLSLLAKF RSASLHSEPL MPHNATYPDS
FQQPPCSALP PSPSHAFSQS PCTASYPHSP GSPSEPESPY QHSVDTPPLP YHATEASETQ
SGQPVDATAD RHVVLSIPNG DFRPVCYEEP QHWCSVAYYE LNNRVGETFQ ASSRSVLIDG
FTDPSNNRNR FCLGLLSNVN RNSTIENTRR HIGKGVHLYY VGGEVYAECV SDSSIFVQSR
NCNYQHGFHP ATVCKIPSGC SLKVFNNQLF AQLLAQSVHH GFEVVYELTK MCTIRMSFVK
GWGAEYHRQD VTSTPCWIEI HLHGPLQWLD KVLTQMGSPH NPISSVS


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