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O15105 (SMAD7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 7

Short name=MAD homolog 7
Short name=Mothers against DPP homolog 7
Alternative name(s):
Mothers against decapentaplegic homolog 8
Short name=MAD homolog 8
Short name=Mothers against DPP homolog 8
SMAD family member 7
Short name=SMAD 7
Short name=Smad7
Short name=hSMAD7
Gene names
Name:SMAD7
Synonyms:MADH7, MADH8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator By similarity. Ref.10 Ref.13 Ref.16 Ref.19 Ref.23

Subunit structure

Interacts with WWP1 By similarity. Interacts with COPS5. Interacts with NEDD4L. Interacts with STAMBP. Interacts with RNF111, AXIN1 and AXIN2. Interacts with PPP1R15A. Interacts (via MH2 domain) with EP300. Interacts with ACVR1B, SMURF1, SMURF2 and TGFBR1; SMAD7 recruits SMURF1 and SMURF2 to the TGF-beta receptor and regulates its degradation. Interacts with PDPK1 (via PH domain). Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Subcellular location

Nucleus. Cytoplasm. Note: Interaction with NEDD4L or RNF111 or induces translocation from the nucleus to the cytoplasm. TGF-beta stimulates its translocation from the nucleus to the cytoplasm. PDPK1 inhibits its translocation from the nucleus to the cytoplasm in response to TGF-beta. Ref.18 Ref.22 Ref.23

Tissue specificity

Ubiquitous with higher expression in the lung and vascular endothelium.

Induction

By TGFB1.

Post-translational modification

Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription By similarity. Phosphorylated by PDPK1. Ref.23

Ubiquitinated by WWP1 By similarity. Polyubiquitinated by RNF111, which is enhanced by AXIN1 and promotes proteasomal degradation. In response to TGF-beta, ubiquitinated by SMURF1; which promotes its degradation. Ref.15 Ref.17 Ref.18 Ref.22

Acetylation prevents ubiquitination and degradation mediated by SMURF1. Ref.17

Involvement in disease

Colorectal cancer 3 (CRCS3) [MIM:612229]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.25

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 componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Traceable author statement. Source: Reactome

adherens junction assembly

Inferred from mutant phenotype PubMed 18593713. Source: BHF-UCL

artery morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular protein complex localization

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

cellular response to transforming growth factor beta stimulus

Inferred from mutant phenotype PubMed 18593713. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

negative regulation of BMP signaling pathway

Inferred from direct assay PubMed 17438144. Source: BHF-UCL

negative regulation of cell migration

Traceable author statement PubMed 19018011. Source: BHF-UCL

negative regulation of epithelial to mesenchymal transition

Traceable author statement PubMed 19018011. Source: BHF-UCL

negative regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 17438144. Source: BHF-UCL

negative regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

negative regulation of peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

negative regulation of protein ubiquitination

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17438144. Source: BHF-UCL

negative regulation of transcription by competitive promoter binding

Inferred from direct assay PubMed 17438144. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17438144. Source: BHF-UCL

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 12151385PubMed 17438144PubMed 18762808. Source: BHF-UCL

negative regulation of ubiquitin-protein transferase activity

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

pathway-restricted SMAD protein phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell-cell adhesion

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.15. Source: BHF-UCL

positive regulation of protein ubiquitination

Inferred from direct assay PubMed 16720724. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

protein stabilization

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

regulation of activin receptor signaling pathway

Inferred from direct assay PubMed 16720724. Source: BHF-UCL

regulation of cardiac muscle contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of transforming growth factor beta receptor signaling pathway

Inferred by curator PubMed 18952608. Source: BHF-UCL

regulation of ventricular cardiac muscle cell membrane depolarization

Inferred by curator PubMed 18952608. Source: BHF-UCL

response to laminar fluid shear stress

Inferred from expression pattern Ref.2. Source: BHF-UCL

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle tissue morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

ventricular septum morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay Ref.15PubMed 17438144. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.15PubMed 12151385PubMed 17438144. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 12151385. Source: BHF-UCL

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 Ref.2. Source: BHF-UCL

activin binding

Inferred from physical interaction PubMed 16720724. Source: BHF-UCL

beta-catenin binding

Inferred from physical interaction PubMed 18593713. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 22344298. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription regulatory region DNA binding

Inferred from direct assay PubMed 17438144. Source: BHF-UCL

transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity

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

type I transforming growth factor beta receptor binding

Inferred from physical interaction Ref.15. Source: BHF-UCL

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 12151385. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15105-1)

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 2 (identifier: O15105-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-215: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O15105-3)

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Mothers against decapentaplegic homolog 7
PRO_0000090872

Regions

Domain64 – 207144MH1
Domain261 – 426166MH2
Region208 – 21710Important for interaction with SMURF2
Motif208 – 2114PY-motif
Compositional bias27 – 359Poly-Gly
Compositional bias49 – 568Poly-Gly
Compositional bias207 – 2104Poly-Pro

Sites

Metal binding1251Zinc By similarity
Metal binding1801Zinc By similarity
Metal binding1921Zinc By similarity
Metal binding1971Zinc By similarity

Amino acid modifications

Modified residue641N6-acetyllysine; alternate Ref.17
Modified residue701N6-acetyllysine; alternate Ref.17
Modified residue2491Phosphoserine By similarity
Cross-link64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.17
Cross-link70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.17

Natural variations

Alternative sequence1 – 215215Missing in isoform 2.
VSP_045197
Alternative sequence2231Missing in isoform 3.
VSP_047540

Experimental info

Mutagenesis641K → A: Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-70. Ref.17
Mutagenesis701K → A: Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-64. Ref.17
Mutagenesis207 – 2115Missing: Diminishes interaction with SMURF2. Ref.13
Mutagenesis2111Y → A: Diminishes interaction with SMURF2 and reduces inhibition of TGF-beta signaling. Ref.13
Mutagenesis409 – 42618Missing: 90% reduction in TGF-beta receptor binding. Ref.1
Sequence conflict711G → C in AAB81354. Ref.3

Secondary structure

..... 426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 5B76EC986776C102

FASTA42646,426
        10         20         30         40         50         60 
MFRTKRSALV RRLWRSRAPG GEDEEEGAGG GGGGGELRGE GATDSRAHGA GGGGPGRAGC 

        70         80         90        100        110        120 
CLGKAVRGAK GHHHPHPPAA GAGAAGGAEA DLKALTHSVL KKLKERQLEL LLQAVESRGG 

       130        140        150        160        170        180 
TRTACLLLPG RLDCRLGPGA PAGAQPAQPP SSYSLPLLLC KVFRWPDLRH SSEVKRLCCC 

       190        200        210        220        230        240 
ESYGKINPEL VCCNPHHLSR LCELESPPPP YSRYPMDFLK PTADCPDAVP SSAETGGTNY 

       250        260        270        280        290        300 
LAPGGLSDSQ LLLEPGDRSH WCVVAYWEEK TRVGRLYCVQ EPSLDIFYDL PQGNGFCLGQ 

       310        320        330        340        350        360 
LNSDNKSQLV QKVRSKIGCG IQLTREVDGV WVYNRSSYPI FIKSATLDNP DSRTLLVHKV 

       370        380        390        400        410        420 
FPGFSIKAFD YEKAYSLQRP NDHEFMQQPW TGFTVQISFV KGWGQCYTRQ FISSCPCWLE 


VIFNSR 

« Hide

Isoform 2 [UniParc].

Checksum: 04F71C0D2D257D71
Show »

FASTA21123,901
Isoform 3 [UniParc].

Checksum: 881EA3C25C342A91
Show »

FASTA42546,355

References

« Hide 'large scale' references
[1]"The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling."
Hayashi H., Abdollah S., Qiu Y., Cai J., Xu Y.-Y., Grinnell B.W., Richardson M.A., Topper J.N., Gimbrone M.A. Jr., Wrana J.L., Falb D.
Cell 89:1165-1173(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF 409-ARG--ARG-426.
Tissue: Umbilical vein endothelial cell.
[2]"Vascular MADs: two novel MAD-related genes selectively inducible by flow in human vascular endothelium."
Topper J.N., Cai J., Qui Y., Anderson K.R., Xu Y.-Y., Deeds J.D., Feeley R., Gimeno C.J., Woolf E.A., Tayber O., Mays G.G., Sampson B.A., Schoen F.J., Gimbrone M.A. Jr., Falb D.
Proc. Natl. Acad. Sci. U.S.A. 94:9314-9319(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Umbilical vein endothelial cell.
[3]"Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling."
Nakao A., Afrakhte M., Moren A., Nakayama T., Christian J.L., Heuchel R., Itoh S., Kawabata M., Heldin N.-E., Heldin C.-H., ten Dijke P.
Nature 389:631-635(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[4]Hagiwara K., Yang K., McMenamin M.G., Freeman A.H., Bennett W.P., Nagashima M., Minter A.R., Miyazono K., Takenoshita S., Harris C.C.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-271 (ISOFORM 3).
Tissue: Pulmonary artery.
[6]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Lung.
[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]"Roles of pathway-specific and inhibitory Smads in activin receptor signaling."
Lebrun J.J., Takabe K., Chen Y., Vale W.
Mol. Endocrinol. 13:15-23(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACVR1B, FUNCTION.
[11]"The Smad pathway."
Wrana J.L., Attisano L.
Cytokine Growth Factor Rev. 11:5-13(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"TGF-beta signaling by Smad proteins."
Miyazono K.
Cytokine Growth Factor Rev. 11:15-22(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-beta receptor for degradation."
Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L.
Mol. Cell 6:1365-1375(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-211 AND 207-PRO--TYR-211, INTERACTION WITH SMURF2 AND TGFBR1.
[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]"Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMURF1 AND TGFBR1, PROTEASOMAL DEGRADATION.
[16]"Phosphorylation regulation of the interaction between Smad7 and activin type I receptor."
Liu X., Nagarajan R.P., Vale W., Chen Y.
FEBS Lett. 519:93-98(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACVR1B, FUNCTION.
[17]"Control of Smad7 stability by competition between acetylation and ubiquitination."
Gronroos E., Hellman U., Heldin C.H., Ericsson J.
Mol. Cell 10:483-493(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EP300, ACETYLATION AT LYS-64 AND LYS-70, UBIQUITINATION AT LYS-64 AND LYS-70, MUTAGENESIS OF LYS-64 AND LYS-70.
[18]"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, UBIQUITINATION, SUBCELLULAR LOCATION.
[19]"GADD34-PP1c recruited by Smad7 dephosphorylates TGFbeta type I receptor."
Shi W., Sun C., He B., Xiong W., Shi X., Yao D., Cao X.
J. Cell Biol. 164:291-300(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP1R15A.
[20]"Jab1/CSN5, a component of the COP9 signalosome, regulates transforming growth factor beta signaling by binding to Smad7 and promoting its degradation."
Kim B.-C., Lee H.-J., Park S.H., Lee S.R., Karpova T.S., McNally J.G., Felici A., Lee D.K., Kim S.-J.
Mol. Cell. Biol. 24:2251-2262(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPS5.
[21]"Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain."
Ogunjimi A.A., Briant D.J., Pece-Barbara N., Le Roy C., Di Guglielmo G.M., Kavsak P., Rasmussen R.K., Seet B.T., Sicheri F., Wrana J.L.
Mol. Cell 19:297-308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMURF2.
[22]"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 AND AXIN2, UBIQUITINATION, SUBCELLULAR LOCATION.
[23]"3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth factor-beta-induced signaling in a kinase-dependent manner through physical interaction with Smad proteins."
Seong H.A., Jung H., Kim K.T., Ha H.
J. Biol. Chem. 282:12272-12289(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY PDPK1, INTERACTION WITH PDPK1.
[24]"An expanded WW domain recognition motif revealed by the interaction between Smad7 and the E3 ubiquitin ligase Smurf2."
Chong P.A., Lin H., Wrana J.L., Forman-Kay J.D.
J. Biol. Chem. 281:17069-17075(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 203-217 IN COMPLEX WITH SMURF2.
[25]"A genome-wide association study shows that common alleles of SMAD7 influence colorectal cancer risk."
Members of the CORGI consortium
Broderick P., Carvajal-Carmona L., Pittman A.M., Webb E., Howarth K., Rowan A., Lubbe S., Spain S., Sullivan K., Fielding S., Jaeger E., Vijayakrishnan J., Kemp Z., Gorman M., Chandler I., Papaemmanuil E., Penegar S., Wood W. expand/collapse author list , Sellick G., Qureshi M., Teixeira A., Domingo E., Barclay E., Martin L., Sieber O., Kerr D., Gray R., Peto J., Cazier J.-B., Tomlinson I., Houlston R.S.
Nat. Genet. 39:1315-1317(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CRCS3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF010193 mRNA. Translation: AAB81246.1.
AF015261 mRNA. Translation: AAB81354.1.
AF026559 expand/collapse EMBL AC list , AF026556, AF026557, AF026558 Genomic DNA. Translation: AAL68977.1.
AK301535 mRNA. Translation: BAH13509.1.
DA882147 mRNA. No translation available.
AC114684 Genomic DNA. No translation available.
BC074818 mRNA. Translation: AAH74818.2.
BC074819 mRNA. Translation: AAH74819.2.
CCDSCCDS11936.1. [O15105-1]
CCDS54186.1. [O15105-2]
CCDS59317.1. [O15105-3]
RefSeqNP_001177750.1. NM_001190821.1. [O15105-3]
NP_001177751.1. NM_001190822.1. [O15105-2]
NP_001177752.1. NM_001190823.1.
NP_005895.1. NM_005904.3. [O15105-1]
UniGeneHs.465087.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJYNMR-B203-217[»]
2KXQNMR-B203-217[»]
2LTVNMR-B206-217[»]
2LTWNMR-B205-217[»]
2LTXNMR-B203-217[»]
2LTYNMR-B203-217[»]
2LTZNMR-B203-217[»]
ProteinModelPortalO15105.
SMRO15105. Positions 112-201, 261-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110267. 86 interactions.
DIPDIP-42252N.
IntActO15105. 26 interactions.
MINTMINT-1179821.
STRING9606.ENSP00000262158.

PTM databases

PhosphoSiteO15105.

Proteomic databases

PaxDbO15105.
PRIDEO15105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262158; ENSP00000262158; ENSG00000101665. [O15105-1]
ENST00000589634; ENSP00000467621; ENSG00000101665. [O15105-3]
ENST00000591805; ENSP00000466902; ENSG00000101665. [O15105-2]
GeneID4092.
KEGGhsa:4092.
UCSCuc002ldg.3. human. [O15105-1]

Organism-specific databases

CTD4092.
GeneCardsGC18M046446.
HGNCHGNC:6773. SMAD7.
HPACAB026212.
HPA028897.
MIM602932. gene.
612229. phenotype.
neXtProtNX_O15105.
PharmGKBPA134875286.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309572.
HOGENOMHOG000060106.
HOVERGENHBG053021.
InParanoidO15105.
KOK04677.
OMAGQLCSEN.
OrthoDBEOG7GN2PK.
PhylomeDBO15105.
TreeFamTF314923.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkO15105.

Gene expression databases

ArrayExpressO15105.
BgeeO15105.
CleanExHS_SMAD7.
GenevestigatorO15105.

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. 2 hits.
PROSITEPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO15105.
GeneWikiMothers_against_decapentaplegic_homolog_7.
GenomeRNAi4092.
NextBio16046.
PROO15105.
SOURCESearch...

Entry information

Entry nameSMAD7_HUMAN
AccessionPrimary (citable) accession number: O15105
Secondary accession number(s): B7Z773 expand/collapse secondary AC list , K7EQ10, O14740, Q6DK23
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 150 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM