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O43541 (SMAD6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mothers against decapentaplegic homolog 6

Short name=MAD homolog 6
Short name=Mothers against DPP homolog 6
Alternative name(s):
SMAD family member 6
Short name=SMAD 6
Short name=Smad6
Short name=hSMAD6
Gene names
Name:SMAD6
Synonyms:MADH6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.13 Ref.17 Ref.18

Subunit structure

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. Ref.2 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Nucleus Ref.18.

Tissue specificity

Ubiquitous in various organs, with higher levels in lung. Isoform B is up-regulated in diseased heart tissue.

Post-translational modification

Phosphorylated by BMP type 1 receptor kinase and by PRKX. Ref.18

Ubiquitinated by WWP1 By similarity. 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. Ref.20

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 By similarity.

Involvement in 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.
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 (Ref.19). Ref.19

Sequence similarities

Belongs to the dwarfin/SMAD family.

Contains 1 MH1 (MAD homology 1) domain.

Contains 1 MH2 (MAD homology 2) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandDNA-binding
Metal-binding
Zinc
   PTMIsopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Traceable author statement. Source: Reactome

cell-substrate adhesion

Inferred from mutant phenotype Ref.18. Source: UniProtKB

immune response

Inferred from mutant phenotype PubMed 16886151. Source: BHF-UCL

intracellular signal transduction

Inferred from direct assay PubMed 9256479. Source: GOC

negative regulation of BMP signaling pathway

Inferred from direct assay Ref.2. Source: BHF-UCL

negative regulation of SMAD protein complex assembly

Inferred from direct assay Ref.2. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 19047146. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 19047146. Source: BHF-UCL

negative regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay Ref.2. Source: BHF-UCL

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 19047146. Source: BHF-UCL

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to laminar fluid shear stress

Inferred from expression pattern PubMed 9256479. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

zygotic specification of dorsal/ventral axis

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

   Cellular_componentcytoplasm

Traceable author statement PubMed 19018011. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.18. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 23610558. Source: MGI

transcription factor complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionI-SMAD binding

Inferred from physical interaction PubMed 9256479. Source: BHF-UCL

R-SMAD binding

Inferred from physical interaction PubMed 9256479Ref.2. Source: BHF-UCL

chromatin binding

Inferred from direct assay Ref.18. Source: UniProtKB

co-SMAD binding

Inferred from physical interaction PubMed 9256479. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16299379Ref.18Ref.14. Source: IntAct

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription regulatory region DNA binding

Inferred from direct assay Ref.18. Source: UniProtKB

transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity

Inferred from direct assay PubMed 9256479. Source: BHF-UCL

type I activin receptor binding

Inferred from direct assay Ref.2. Source: BHF-UCL

type I transforming growth factor beta receptor binding

Inferred from direct assay Ref.2. Source: BHF-UCL

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 11278251. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: O43541-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: O43541-2)

Also known as: Smad 6S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-261: Missing.
     262-273: NPYHFSRLCGPE → MSRMGKPIETQK
Isoform D (identifier: O43541-4)

The sequence of this isoform differs from the canonical sequence as follows:
     318-338: DASMSPDATKPSHWCSVAYWE → AADAGIGSRGNRGLESSVPCS
     339-496: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Mothers against decapentaplegic homolog 6
PRO_0000090869

Regions

Domain148 – 275128MH1
Domain331 – 496166MH2
Compositional bias25 – 339Poly-Gly
Compositional bias82 – 854Poly-Arg
Compositional bias165 – 1684Poly-Leu
Compositional bias251 – 2544Poly-Ala
Compositional bias275 – 2784Poly-Pro

Sites

Metal binding2051Zinc By similarity
Metal binding2471Zinc By similarity
Metal binding2601Zinc By similarity
Metal binding2651Zinc By similarity

Amino acid modifications

Modified residue751Dimethylated arginine; alternate By similarity
Modified residue751Omega-N-methylarginine; alternate By similarity
Modified residue821Dimethylated arginine; alternate By similarity
Modified residue821Omega-N-methylarginine; alternate By similarity
Modified residue4351Phosphoserine; by PRKX; in vitro Ref.18
Cross-link173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20

Natural variations

Alternative sequence1 – 261261Missing in isoform B.
VSP_006179
Alternative sequence262 – 27312NPYHF…LCGPE → MSRMGKPIETQK in isoform B.
VSP_006180
Alternative sequence318 – 33821DASMS…VAYWE → AADAGIGSRGNRGLESSVPC S in isoform D.
VSP_035489
Alternative sequence339 – 496158Missing in isoform D.
VSP_035490
Natural variant3251A → T Found in a patient with congenital mitral valve prolapse. Ref.19
Corresponds to variant rs199822239 [ dbSNP | Ensembl ].
VAR_068074
Natural variant4151P → L in AOVD2; results in significantly lower activity than wild-type in inhibiting BMP signaling in a transcriptional reporter assay. Ref.19
VAR_068075
Natural variant4841C → F in AOVD2; results in significantly lower activity than wild-type in inhibiting BMP signaling in a transcriptional reporter assay. Ref.19
VAR_068076

Experimental info

Mutagenesis1731K → R: Abolishes monoubiquitination by UBE2O. Ref.20
Mutagenesis4351S → A: Loss of in vitro phosphorylation by PRKX. Ref.18
Mutagenesis4711G → S: Loss of SMAD1-binding and of inhibition of BMP-SMAD1 signaling. No effect on interaction with BMPR1B and TGFBR1. Ref.2
Mutagenesis478 – 49619Missing: Loss of interaction with BMPR1B, TGFBR1 and SMAD1. Ref.2
Sequence conflict211D → N in AAB94137. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: A4B928AE2D34EBC2

FASTA49653,497
        10         20         30         40         50         60 
MFRSKRSGLV RRLWRSRVVP DREEGGSGGG GGGDEDGSLG SRAEPAPRAR EGGGCGRSEV 

        70         80         90        100        110        120 
RPVAPRRPRD AVGQRGAQGA GRRRRAGGPP RPMSEPGAGA GSSLLDVAEP GGPGWLPESD 

       130        140        150        160        170        180 
CETVTCCLFS ERDAAGAPRD ASDPLAGAAL EPAGGGRSRE ARSRLLLLEQ ELKTVTYSLL 

       190        200        210        220        230        240 
KRLKERSLDT LLEAVESRGG VPGGCVLVPR ADLRLGGQPA PPQLLLGRLF RWPDLQHAVE 

       250        260        270        280        290        300 
LKPLCGCHSF AAAADGPTVC CNPYHFSRLC GPESPPPPYS RLSPRDEYKP LDLSDSTLSY 

       310        320        330        340        350        360 
TETEATNSLI TAPGEFSDAS MSPDATKPSH WCSVAYWEHR TRVGRLYAVY DQAVSIFYDL 

       370        380        390        400        410        420 
PQGSGFCLGQ LNLEQRSESV RRTRSKIGFG ILLSKEPDGV WAYNRGEHPI FVNSPTLDAP 

       430        440        450        460        470        480 
GGRALVVRKV PPGYSIKVFD FERSGLQHAP EPDAADGPYD PNSVRISFAK GWGPCYSRQF 

       490 
ITSCPCWLEI LLNNPR 

« Hide

Isoform B (Smad 6S) [UniParc].

Checksum: 0847C2C84DC0B2A2
Show »

FASTA23526,236
Isoform D [UniParc].

Checksum: C4D02353D7FD76CE
Show »

FASTA33835,467

References

« Hide 'large scale' references
[1]"Mad-related genes in the human."
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.
Nat. Genet. 13:347-349(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[2]"Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor."
Hata A., Lagna G., Massague J., Hemmati-Brivanlou A.
Genes Dev. 12:186-197(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH ACVR1B; BMPR1B; SMAD1 AND TGFBR1, MUTAGENESIS OF GLY-471 AND 478-ARG--ARG-496.
Tissue: T-cell.
[3]"Induction of inhibitory Smad6 and Smad7 mRNA by TGF-beta family members."
Afrakhte M., Moren A., Jossan S., Itoh S., Sampath K., Westermark B., Heldin C.H., Heldin N.E., ten Dijke P.
Biochem. Biophys. Res. Commun. 249:505-511(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Placenta.
[4]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
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
[5]"Identification of a new SMAD6 variant in human."
Konrad L., Scheiber J.A., Brandt H., Eickelberg O., Hofmann R.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
Tissue: Prostatic carcinoma.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Uterus.
[7]"Determination of the genomic structure of human Smad3, Smad6 and Smad7 and the cloning of the human Smad3 promoter."
Hagiwara K., Freeman A.A.H., McMenamin M.G., Bennett W.P., Yang K., Takenoshita S., Harris C.C.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B).
[8]"TGF-beta signal transduction."
Massague J.
Annu. Rev. Biochem. 67:753-791(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[9]"Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells."
Verschueren K., Huylebroeck D.
Cytokine Growth Factor Rev. 10:187-199(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[10]"The Smad pathway."
Wrana J.L., Attisano L.
Cytokine Growth Factor Rev. 11:5-13(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"TGF-beta signaling by Smad proteins."
Miyazono K.
Cytokine Growth Factor Rev. 11:15-22(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Smad6 as a transcriptional corepressor."
Bai S., Shi X., Yang X., Cao X.
J. Biol. Chem. 275:8267-8270(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOXC8.
[13]"Human truncated Smad 6 (Smad 6s) inhibits the BMP pathway in Xenopus laevis."
Krishnan P., King M.W., Neff A.W., Sandusky G.E., Bierman K.L., Grinnell B., Smith R.C.
Dev. Growth Differ. 43:115-132(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM B).
[14]"Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads."
Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S.
EMBO J. 20:4132-4142(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STAMBP.
[15]"Arkadia amplifies TGF-beta superfamily signaling through degradation of Smad7."
Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A., Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.
EMBO J. 22:6458-6470(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF111.
[16]"Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
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.
EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXIN1.
[17]"Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor signaling through direct interaction with the adaptor Pellino-1."
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.
Nat. Immunol. 7:1057-1065(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PELI1.
[18]"Smad6 is a protein kinase X phosphorylation substrate and is required for HL-60 cell differentiation."
Glesne D., Huberman E.
Oncogene 25:4086-4098(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKX, MUTAGENESIS OF SER-435, PHOSPHORYLATION AT SER-435.
[19]"Nonsynonymous variants in the SMAD6 gene predispose to congenital cardiovascular malformation."
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.
Hum. Mutat. 33:720-727(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CONGENITAL CARDIOVASCULAR MALFORMATIONS, VARIANT THR-325, VARIANTS AOVD2 LEU-415 AND PHE-484, CHARACTERIZATION OF VARIANTS AOVD2 LEU-415 AND PHE-484.
[20]"Fine-tuning BMP7 signalling in adipogenesis by UBE2O/E2-230K-mediated monoubiquitination of SMAD6."
Zhang X., Zhang J., Bauer A., Zhang L., Selinger D.W., Lu C.X., Ten Dijke P.
EMBO J. 32:996-1007(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-173, MUTAGENESIS OF LYS-173.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59914 mRNA. Translation: AAC50792.1.
AF035528 mRNA. Translation: AAB94137.1.
AF043640 mRNA. Translation: AAC00497.1.
AF037469 mRNA. Translation: AAC82331.1.
AF041065 expand/collapse EMBL AC list , AF041062, AF041063, AF041064 Genomic DNA. Translation: AAF14343.1.
AM909653 mRNA. Translation: CAP20377.1.
BC012986 mRNA. Translation: AAH12986.1.
AF101474 Genomic DNA. Translation: AAF06841.1.
CCDSCCDS10221.1. [O43541-1]
CCDS45287.1. [O43541-2]
RefSeqNP_001136333.1. NM_001142861.2. [O43541-2]
NP_005576.3. NM_005585.4. [O43541-1]
UniGeneHs.153863.

3D structure databases

ProteinModelPortalO43541.
SMRO43541. Positions 192-269, 328-493.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110266. 37 interactions.
DIPDIP-36708N.
IntActO43541. 10 interactions.
MINTMINT-1198639.
STRING9606.ENSP00000288840.

PTM databases

PhosphoSiteO43541.

Proteomic databases

MaxQBO43541.
PaxDbO43541.
PRIDEO43541.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288840; ENSP00000288840; ENSG00000137834. [O43541-1]
ENST00000338426; ENSP00000345054; ENSG00000137834. [O43541-2]
ENST00000457357; ENSP00000396961; ENSG00000137834. [O43541-4]
ENST00000557916; ENSP00000452955; ENSG00000137834. [O43541-4]
GeneID4091.
KEGGhsa:4091.
UCSCuc002aqf.3. human. [O43541-1]
uc002aqg.3. human. [O43541-2]

Organism-specific databases

CTD4091.
GeneCardsGC15P066994.
H-InvDBHIX0132566.
HGNCHGNC:6772. SMAD6.
MIM602931. gene.
614823. phenotype.
neXtProtNX_O43541.
Orphanet1244. Bicuspid aortic valve.
PharmGKBPA30529.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309572.
HOVERGENHBG053021.
InParanoidO43541.
KOK04677.
OMAWRSRLIP.
OrthoDBEOG7GN2PK.
PhylomeDBO43541.
TreeFamTF314923.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkO43541.

Gene expression databases

ArrayExpressO43541.
BgeeO43541.
CleanExHS_SMAD6.
GenevestigatorO43541.

Family and domain databases

Gene3D2.60.200.10. 1 hit.
3.90.520.10. 2 hits.
InterProIPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERPTHR13703. PTHR13703. 1 hit.
PfamPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 1 hit.
PROSITEPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMAD6. human.
GeneWikiMothers_against_decapentaplegic_homolog_6.
GenomeRNAi4091.
NextBio16042.
PROO43541.
SOURCESearch...

Entry information

Entry nameSMAD6_HUMAN
AccessionPrimary (citable) accession number: O43541
Secondary accession number(s): A9J6M5 expand/collapse secondary AC list , O43654, Q15799, Q7Z7L4, Q96E31, Q9UKZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM