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Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (JV5-1) (SMAD family member 5) (SMAD 5) (Smad5) (hSmad5)

 SMAD5_HUMAN             Reviewed;         465 AA.
Q99717; O14688; Q15798; Q9UQA1;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
22-NOV-2017, entry version 184.
RecName: Full=Mothers against decapentaplegic homolog 5;
Short=MAD homolog 5;
Short=Mothers against DPP homolog 5;
AltName: Full=JV5-1;
AltName: Full=SMAD family member 5;
Short=SMAD 5;
Short=Smad5;
Short=hSmad5;
Name=SMAD5; Synonyms=MADH5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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 [GENOMIC DNA / MRNA].
PubMed=9288787;
Hejlik D.P., Kottickal L.V., Liang H., Fairman J., Davis T.,
Janecki T., Sexton D., Perry W. III, Tavtigian S.V., Teng D.H.,
Nagarajan L.;
"Localization of SMAD5 and its evaluation as a candidate myeloid tumor
suppressor.";
Cancer Res. 57:3779-3783(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9264367; DOI=10.1038/sj.leu.2400750;
Zavadil J., Brezinova J., Svoboda P., Zemanova Z., Michalova K.;
"Smad5, a tumor suppressor candidate at 5q31.1, is hemizygously lost
and not mutated in the retained allele in human leukemia cell line
HL60.";
Leukemia 11:1187-1192(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9484787; DOI=10.1038/sj.onc.1201614;
Gemma A., Hagiwara K., Vincent F., Ke Y., Hancock A.R., Nagashima M.,
Bennett W.P., Harris C.C.;
"hSmad5 gene, a human hSmad family member: its full length cDNA,
genomic structure, promoter region and mutation analysis in human
tumors.";
Oncogene 16:951-956(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF GLY-419.
PubMed=9442019; DOI=10.1074/jbc.273.4.1872;
Nishimura R., Kato Y., Chen D., Harris S.E., Mundy G.R., Yoneda T.;
"Smad5 and DPC4 are key molecules in mediating BMP-2-induced
osteoblastic differentiation of the pluripotent mesenchymal precursor
cell line C2C12.";
J. Biol. Chem. 273:1872-1879(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
PROTEIN SEQUENCE OF 2-16; 34-40; 130-158; 283-306 AND 309-319,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lempens A., Norman J.C.;
Submitted (OCT-2009) to UniProtKB.
[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 ZNF8.
PubMed=12370310; DOI=10.1128/MCB.22.21.7633-7644.2002;
Jiao K., Zhou Y., Hogan B.L.M.;
"Identification of mZnf8, a mouse Kruppel-like transcriptional
repressor, as a novel nuclear interaction partner of Smad1.";
Mol. Cell. Biol. 22:7633-7644(2002).
[13]
INTERACTION WITH SUV39H1 AND SUV39H2.
PubMed=15107829; DOI=10.1038/sj.onc.1207660;
Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M.,
Lechleider R.J.;
"Suv39h histone methyltransferases interact with Smads and cooperate
in BMP-induced repression.";
Oncogene 23:5242-5251(2004).
[14]
INTERACTION WITH LEMD3.
PubMed=15647271; DOI=10.1074/jbc.M411234200;
Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J.,
Zhou S., Luo K.;
"The integral inner nuclear membrane protein MAN1 physically interacts
with the R-Smad proteins to repress signaling by the transforming
growth factor-{beta} superfamily of cytokines.";
J. Biol. Chem. 280:15992-16001(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 AND SER-465, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
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).
-!- FUNCTION: Transcriptional modulator activated by BMP (bone
morphogenetic proteins) type 1 receptor kinase. SMAD5 is a
receptor-regulated SMAD (R-SMAD).
-!- SUBUNIT: May form trimers with the co-SMAD SMAD4. Interacts with
PEBP2-alpha subunit and SMURF1. Interacts with SUV39H1 and
SUV39H2. Interacts (via MH2 domain) with LEMD3. Interacts with
WWP1. Interacts with TMEM119 (By similarity). Interacts with ZNF8
(PubMed:12370310). Interacts with RANBP3L (PubMed:25755279).
{ECO:0000250|UniProtKB:P97454, ECO:0000269|PubMed:12370310,
ECO:0000269|PubMed:15107829, ECO:0000269|PubMed:15647271,
ECO:0000269|PubMed:25755279}.
-!- INTERACTION:
P17844:DDX5; NbExp=3; IntAct=EBI-6391136, EBI-351962;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in the
absence of ligand. Migrates to the nucleus when complexed with
SMAD4.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins)
type 1 receptor kinase.
-!- PTM: Ubiquitin-mediated proteolysis by SMAD-specific E3 ubiquitin
ligase SMURF1.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; U59913; AAC50791.1; -; mRNA.
EMBL; AF010601; AAB66353.1; -; mRNA.
EMBL; AF010607; AAB92396.1; -; Genomic_DNA.
EMBL; AF010602; AAB92396.1; JOINED; Genomic_DNA.
EMBL; AF010603; AAB92396.1; JOINED; Genomic_DNA.
EMBL; AF010604; AAB92396.1; JOINED; Genomic_DNA.
EMBL; AF010605; AAB92396.1; JOINED; Genomic_DNA.
EMBL; AF010606; AAB92396.1; JOINED; Genomic_DNA.
EMBL; U73825; AAB95090.1; -; mRNA.
EMBL; AF009744; AAB82655.1; -; Genomic_DNA.
EMBL; AF009739; AAB82655.1; JOINED; Genomic_DNA.
EMBL; AF009740; AAB82655.1; JOINED; Genomic_DNA.
EMBL; AF009741; AAB82655.1; JOINED; Genomic_DNA.
EMBL; AF009742; AAB82655.1; JOINED; Genomic_DNA.
EMBL; AF009743; AAB82655.1; JOINED; Genomic_DNA.
EMBL; AF009678; AAB72180.1; -; mRNA.
EMBL; BC009682; AAH09682.1; -; mRNA.
CCDS; CCDS75308.1; -.
RefSeq; NP_001001419.1; NM_001001419.2.
RefSeq; NP_001001420.1; NM_001001420.2.
RefSeq; NP_005894.3; NM_005903.6.
RefSeq; XP_016864959.1; XM_017009470.1.
UniGene; Hs.167700; -.
ProteinModelPortal; Q99717; -.
SMR; Q99717; -.
BioGrid; 110265; 62.
DIP; DIP-57571N; -.
IntAct; Q99717; 32.
MINT; MINT-1180224; -.
STRING; 9606.ENSP00000441954; -.
iPTMnet; Q99717; -.
PhosphoSitePlus; Q99717; -.
BioMuta; SMAD5; -.
DMDM; 13959566; -.
EPD; Q99717; -.
MaxQB; Q99717; -.
PaxDb; Q99717; -.
PeptideAtlas; Q99717; -.
PRIDE; Q99717; -.
DNASU; 4090; -.
Ensembl; ENST00000545279; ENSP00000441954; ENSG00000113658.
Ensembl; ENST00000545620; ENSP00000446474; ENSG00000113658.
GeneID; 4090; -.
KEGG; hsa:4090; -.
UCSC; uc032vlw.2; human.
CTD; 4090; -.
DisGeNET; 4090; -.
EuPathDB; HostDB:ENSG00000113658.16; -.
GeneCards; SMAD5; -.
HGNC; HGNC:6771; SMAD5.
HPA; HPA058931; -.
MIM; 603110; gene.
neXtProt; NX_Q99717; -.
OpenTargets; ENSG00000113658; -.
PharmGKB; PA30528; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOVERGEN; HBG053353; -.
InParanoid; Q99717; -.
KO; K16790; -.
OMA; DVQPVEY; -.
OrthoDB; EOG091G082C; -.
PhylomeDB; Q99717; -.
Reactome; R-HSA-201451; Signaling by BMP.
SignaLink; Q99717; -.
SIGNOR; Q99717; -.
ChiTaRS; SMAD5; human.
GeneWiki; Mothers_against_decapentaplegic_homolog_5; -.
GenomeRNAi; 4090; -.
PRO; PR:Q99717; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113658; -.
CleanEx; HS_SMAD5; -.
ExpressionAtlas; Q99717; baseline and differential.
Genevisible; Q99717; HS.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0071141; C:SMAD protein complex; NAS:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; NAS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0030618; F:transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; TAS:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0001880; P:Mullerian duct regression; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0002051; P:osteoblast fate commitment; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
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; NAS:UniProtKB.
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;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.7}.
CHAIN 2 465 Mothers against decapentaplegic homolog
5.
/FTId=PRO_0000090865.
DOMAIN 13 137 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 271 465 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
COMPBIAS 40 46 Poly-Lys.
METAL 65 65 Zinc. {ECO:0000250}.
METAL 110 110 Zinc. {ECO:0000250}.
METAL 122 122 Zinc. {ECO:0000250}.
METAL 127 127 Zinc. {ECO:0000250}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.7}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MUTAGEN 419 419 G->S: Loss of phosphorylation.
{ECO:0000269|PubMed:9442019}.
CONFLICT 175 175 D -> H (in Ref. 1; AAC50791).
{ECO:0000305}.
CONFLICT 237 237 N -> P (in Ref. 1; AAC50791).
{ECO:0000305}.
CONFLICT 293 293 S -> R (in Ref. 1; AAC50791).
{ECO:0000305}.
SEQUENCE 465 AA; 52258 MW; 4A1FD7EC7BD06728 CRC64;
MTSMASLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME ELEKALSSPG
QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS HHELKPLDIC EFPFGSKQKE
VCINPYHYKR VESPVLPPVL VPRHNEFNPQ HSLLVQFRNL SHNEPHMPQN ATFPDSFHQP
NNTPFPLSPN SPYPPSPASS TYPNSPASSG PGSPFQLPAD TPPPAYMPPD DQMGQDNSQP
MDTSNNMIPQ IMPSISSRDV QPVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
DPSNNKSRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD SSIFVQSRNC
NFHHGFHPTT VCKIPSSCSL KIFNNQEFAQ LLAQSVNHGF EAVYELTKMC TIRMSFVKGW
GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPLNP ISSVS


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E2186m Dwarfin-C,Dwf-C,MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Mouse,mSmad5,Msmad5,Mus musculus,SMAD 5,SMAD family member 5,Smad5,Smad5
U0647h CLIA BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 1,Smad 96T
U2186c CLIA Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
E2186c ELISA kit Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
U2186c CLIA kit Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
E2186c ELISA Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
E2186c Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5
EIAAB38719 Deletion target in pancreatic carcinoma 4 homolog,Dpc4,MAD homolog 4,Madh4,Mothers against decapentaplegic homolog 4,Mothers against DPP homolog 4,Mouse,Mus musculus,SMAD 4,SMAD family member 4,Smad4,
E0647h ELISA BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 1,Sma 96T
E0647h ELISA kit BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 96T
U2184h CLIA kit hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Sm 96T


 

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