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O15105

- SMAD7_HUMAN

UniProt

O15105 - SMAD7_HUMAN

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Protein

Mothers against decapentaplegic homolog 7

Gene

SMAD7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi125 – 1251ZincBy similarity
Metal bindingi180 – 1801ZincBy similarity
Metal bindingi192 – 1921ZincBy similarity
Metal bindingi197 – 1971ZincBy similarity

GO - Molecular functioni

  1. activin binding Source: BHF-UCL
  2. beta-catenin binding Source: BHF-UCL
  3. I-SMAD binding Source: BHF-UCL
  4. metal ion binding Source: UniProtKB-KW
  5. sequence-specific DNA binding transcription factor activity Source: InterPro
  6. transcription regulatory region DNA binding Source: BHF-UCL
  7. transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity Source: BHF-UCL
  8. type I transforming growth factor beta receptor binding Source: BHF-UCL
  9. ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  1. adherens junction assembly Source: BHF-UCL
  2. artery morphogenesis Source: BHF-UCL
  3. BMP signaling pathway Source: Reactome
  4. cellular protein complex localization Source: BHF-UCL
  5. cellular response to transforming growth factor beta stimulus Source: BHF-UCL
  6. gene expression Source: Reactome
  7. negative regulation of BMP signaling pathway Source: BHF-UCL
  8. negative regulation of cell migration Source: BHF-UCL
  9. negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  10. negative regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  11. negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  12. negative regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
  13. negative regulation of protein ubiquitination Source: BHF-UCL
  14. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  15. negative regulation of transcription by competitive promoter binding Source: BHF-UCL
  16. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  17. negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  18. negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  19. pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  20. positive regulation of cell-cell adhesion Source: BHF-UCL
  21. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  22. positive regulation of protein ubiquitination Source: BHF-UCL
  23. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
  24. protein stabilization Source: BHF-UCL
  25. regulation of activin receptor signaling pathway Source: BHF-UCL
  26. regulation of cardiac muscle contraction Source: BHF-UCL
  27. regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  28. regulation of ventricular cardiac muscle cell membrane depolarization Source: BHF-UCL
  29. response to laminar fluid shear stress Source: BHF-UCL
  30. transcription, DNA-templated Source: Reactome
  31. transcription initiation from RNA polymerase II promoter Source: Reactome
  32. transforming growth factor beta receptor signaling pathway Source: Reactome
  33. ureteric bud development Source: Ensembl
  34. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
  35. ventricular septum morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_12034. Signaling by BMP.
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
SignaLinkiO15105.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SMAD7
Synonyms:MADH7, MADH8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:6773. SMAD7.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: BHF-UCL
  5. plasma membrane Source: BHF-UCL
  6. protein complex Source: MGI
  7. transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641K → A: Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-70. 1 Publication
Mutagenesisi70 – 701K → A: Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-64. 1 Publication
Mutagenesisi207 – 2115Missing: Diminishes interaction with SMURF2. 1 Publication
Mutagenesisi211 – 2111Y → A: Diminishes interaction with SMURF2 and reduces inhibition of TGF-beta signaling. 1 Publication
Mutagenesisi409 – 42618Missing: 90% reduction in TGF-beta receptor binding. 1 PublicationAdd
BLAST

Organism-specific databases

MIMi612229. phenotype.
PharmGKBiPA134875286.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Mothers against decapentaplegic homolog 7PRO_0000090872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641N6-acetyllysine; alternate1 Publication
Cross-linki64 – 64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei70 – 701N6-acetyllysine; alternate1 Publication
Cross-linki70 – 70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei249 – 2491PhosphoserinePROSITE-ProRule annotation

Post-translational modificationi

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.By similarity1 Publication
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.By similarity
Acetylation prevents ubiquitination and degradation mediated by SMURF1.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO15105.
PRIDEiO15105.

PTM databases

PhosphoSiteiO15105.

Expressioni

Tissue specificityi

Ubiquitous with higher expression in the lung and vascular endothelium.

Inductioni

By TGFB1.

Gene expression databases

BgeeiO15105.
CleanExiHS_SMAD7.
ExpressionAtlasiO15105. baseline and differential.
GenevestigatoriO15105.

Organism-specific databases

HPAiCAB026212.
HPA028897.

Interactioni

Subunit structurei

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).By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACVR1BP368962EBI-3861591,EBI-1384128
AXIN1O151698EBI-3861591,EBI-710484
COPS5Q9290510EBI-3861591,EBI-594661
FKBP1AP629423EBI-3861591,EBI-1027571
Rnf111Q99ML92EBI-3861591,EBI-646015From a different organism.
WWP2O003085EBI-3861591,EBI-743923

Protein-protein interaction databases

BioGridi110267. 86 interactions.
DIPiDIP-42252N.
IntActiO15105. 26 interactions.
MINTiMINT-1179821.
STRINGi9606.ENSP00000262158.

Structurei

Secondary structure

1
426
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi204 – 2063Combined sources
Beta strandi212 – 2143Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJYNMR-B203-217[»]
2KXQNMR-B203-217[»]
2LTVNMR-B206-217[»]
2LTWNMR-B205-217[»]
2LTXNMR-B203-217[»]
2LTYNMR-B203-217[»]
2LTZNMR-B203-217[»]
ProteinModelPortaliO15105.
SMRiO15105. Positions 112-201, 261-424.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15105.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 207144MH1PROSITE-ProRule annotationAdd
BLAST
Domaini261 – 426166MH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni208 – 21710Important for interaction with SMURF2

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi208 – 2114PY-motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 359Poly-Gly
Compositional biasi49 – 568Poly-Gly
Compositional biasi207 – 2104Poly-Pro

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.Curated
Contains 1 MH1 (MAD homology 1) domain.PROSITE-ProRule annotation
Contains 1 MH2 (MAD homology 2) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG309572.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000060106.
HOVERGENiHBG053021.
InParanoidiO15105.
KOiK04677.
OMAiGQLCSEN.
OrthoDBiEOG7GN2PK.
PhylomeDBiO15105.
TreeFamiTF314923.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.520.10. 2 hits.
InterProiIPR013790. 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]
PANTHERiPTHR13703. PTHR13703. 1 hit.
PfamiPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTiSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15105-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MFRTKRSALV RRLWRSRAPG GEDEEEGAGG GGGGGELRGE GATDSRAHGA
60 70 80 90 100
GGGGPGRAGC CLGKAVRGAK GHHHPHPPAA GAGAAGGAEA DLKALTHSVL
110 120 130 140 150
KKLKERQLEL LLQAVESRGG TRTACLLLPG RLDCRLGPGA PAGAQPAQPP
160 170 180 190 200
SSYSLPLLLC KVFRWPDLRH SSEVKRLCCC ESYGKINPEL VCCNPHHLSR
210 220 230 240 250
LCELESPPPP YSRYPMDFLK PTADCPDAVP SSAETGGTNY LAPGGLSDSQ
260 270 280 290 300
LLLEPGDRSH WCVVAYWEEK TRVGRLYCVQ EPSLDIFYDL PQGNGFCLGQ
310 320 330 340 350
LNSDNKSQLV QKVRSKIGCG IQLTREVDGV WVYNRSSYPI FIKSATLDNP
360 370 380 390 400
DSRTLLVHKV FPGFSIKAFD YEKAYSLQRP NDHEFMQQPW TGFTVQISFV
410 420
KGWGQCYTRQ FISSCPCWLE VIFNSR
Length:426
Mass (Da):46,426
Last modified:January 1, 1998 - v1
Checksum:i5B76EC986776C102
GO
Isoform 2 (identifier: O15105-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-215: Missing.

Note: No experimental confirmation available.

Show »
Length:211
Mass (Da):23,901
Checksum:i04F71C0D2D257D71
GO
Isoform 3 (identifier: O15105-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: Missing.

Note: No experimental confirmation available.

Show »
Length:425
Mass (Da):46,355
Checksum:i881EA3C25C342A91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711G → C in AAB81354. (PubMed:9335507)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 215215Missing in isoform 2. 1 PublicationVSP_045197Add
BLAST
Alternative sequencei223 – 2231Missing in isoform 3. 1 PublicationVSP_047540

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF010193 mRNA. Translation: AAB81246.1.
AF015261 mRNA. Translation: AAB81354.1.
AF026559
, 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.
CCDSiCCDS11936.1. [O15105-1]
CCDS54186.1. [O15105-2]
CCDS59317.1. [O15105-3]
RefSeqiNP_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]
UniGeneiHs.465087.

Genome annotation databases

EnsembliENST00000262158; ENSP00000262158; ENSG00000101665. [O15105-1]
ENST00000589634; ENSP00000467621; ENSG00000101665. [O15105-3]
ENST00000591805; ENSP00000466902; ENSG00000101665. [O15105-2]
GeneIDi4092.
KEGGihsa:4092.
UCSCiuc002ldg.3. human. [O15105-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF010193 mRNA. Translation: AAB81246.1 .
AF015261 mRNA. Translation: AAB81354.1 .
AF026559
, 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 .
CCDSi CCDS11936.1. [O15105-1 ]
CCDS54186.1. [O15105-2 ]
CCDS59317.1. [O15105-3 ]
RefSeqi NP_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 ]
UniGenei Hs.465087.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DJY NMR - B 203-217 [» ]
2KXQ NMR - B 203-217 [» ]
2LTV NMR - B 206-217 [» ]
2LTW NMR - B 205-217 [» ]
2LTX NMR - B 203-217 [» ]
2LTY NMR - B 203-217 [» ]
2LTZ NMR - B 203-217 [» ]
ProteinModelPortali O15105.
SMRi O15105. Positions 112-201, 261-424.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110267. 86 interactions.
DIPi DIP-42252N.
IntActi O15105. 26 interactions.
MINTi MINT-1179821.
STRINGi 9606.ENSP00000262158.

PTM databases

PhosphoSitei O15105.

Proteomic databases

PaxDbi O15105.
PRIDEi O15105.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262158 ; ENSP00000262158 ; ENSG00000101665 . [O15105-1 ]
ENST00000589634 ; ENSP00000467621 ; ENSG00000101665 . [O15105-3 ]
ENST00000591805 ; ENSP00000466902 ; ENSG00000101665 . [O15105-2 ]
GeneIDi 4092.
KEGGi hsa:4092.
UCSCi uc002ldg.3. human. [O15105-1 ]

Organism-specific databases

CTDi 4092.
GeneCardsi GC18M046446.
HGNCi HGNC:6773. SMAD7.
HPAi CAB026212.
HPA028897.
MIMi 602932. gene.
612229. phenotype.
neXtProti NX_O15105.
PharmGKBi PA134875286.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG309572.
GeneTreei ENSGT00760000119091.
HOGENOMi HOG000060106.
HOVERGENi HBG053021.
InParanoidi O15105.
KOi K04677.
OMAi GQLCSEN.
OrthoDBi EOG7GN2PK.
PhylomeDBi O15105.
TreeFami TF314923.

Enzyme and pathway databases

Reactomei REACT_12034. Signaling by BMP.
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
SignaLinki O15105.

Miscellaneous databases

EvolutionaryTracei O15105.
GeneWikii Mothers_against_decapentaplegic_homolog_7.
GenomeRNAii 4092.
NextBioi 16046.
PROi O15105.
SOURCEi Search...

Gene expression databases

Bgeei O15105.
CleanExi HS_SMAD7.
ExpressionAtlasi O15105. baseline and differential.
Genevestigatori O15105.

Family and domain databases

Gene3Di 2.60.200.10. 1 hit.
3.90.520.10. 2 hits.
InterProi IPR013790. 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 ]
PANTHERi PTHR13703. PTHR13703. 1 hit.
Pfami PF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view ]
SMARTi SM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEi PS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.
    , 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. 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. 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. Cited for: REVIEW.
  12. 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. Cited for: INVOLVEMENT IN CRCS3.

Entry informationi

Entry nameiSMAD7_HUMAN
AccessioniPrimary (citable) accession number: O15105
Secondary accession number(s): B7Z773
, K7EQ10, O14740, Q6DK23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3