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Q62432

- SMAD2_MOUSE

UniProt

Q62432 - SMAD2_MOUSE

Protein

Mothers against decapentaplegic homolog 2

Gene

Smad2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (14 Nov 2006)
      Previous versions | rss
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    Functioni

    Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. 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 bindingi74 – 741ZincBy similarity
    Metal bindingi149 – 1491ZincBy similarity
    Metal bindingi161 – 1611ZincBy similarity
    Metal bindingi166 – 1661ZincBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. double-stranded DNA binding Source: MGI
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. sequence-specific DNA binding transcription factor activity Source: InterPro
    6. SMAD binding Source: UniProtKB
    7. transcription factor binding Source: UniProtKB
    8. transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Source: Ensembl

    GO - Biological processi

    1. anterior/posterior pattern specification Source: MGI
    2. cell fate commitment Source: MGI
    3. common-partner SMAD protein phosphorylation Source: MGI
    4. developmental growth Source: MGI
    5. embryonic cranial skeleton morphogenesis Source: MGI
    6. embryonic foregut morphogenesis Source: MGI
    7. embryonic pattern specification Source: MGI
    8. endoderm development Source: MGI
    9. endoderm formation Source: MGI
    10. gastrulation Source: MGI
    11. heart development Source: MGI
    12. insulin secretion Source: MGI
    13. intracellular signal transduction Source: MGI
    14. in utero embryonic development Source: MGI
    15. lung development Source: MGI
    16. mesoderm formation Source: MGI
    17. negative regulation of cell proliferation Source: Ensembl
    18. negative regulation of transcription, DNA-templated Source: Ensembl
    19. nodal signaling pathway Source: Ensembl
    20. organ growth Source: MGI
    21. palate development Source: BHF-UCL
    22. pancreas development Source: MGI
    23. paraxial mesoderm morphogenesis Source: MGI
    24. pattern specification process Source: MGI
    25. pericardium development Source: MGI
    26. positive regulation of BMP signaling pathway Source: Ensembl
    27. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
    28. positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry Source: Ensembl
    29. positive regulation of transcription, DNA-templated Source: BHF-UCL
    30. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    31. post-embryonic development Source: MGI
    32. protein phosphorylation Source: MGI
    33. regulation of binding Source: MGI
    34. regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    35. response to cholesterol Source: Ensembl
    36. response to glucose Source: MGI
    37. signal transduction involved in regulation of gene expression Source: Ensembl
    38. SMAD protein complex assembly Source: Ensembl
    39. transcription, DNA-templated Source: UniProtKB-KW
    40. transforming growth factor beta receptor signaling pathway Source: MGI
    41. ureteric bud development Source: UniProtKB
    42. zygotic specification of dorsal/ventral axis Source: Ensembl

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_202264. SMAD4 MH2 Domain Mutants in Cancer.
    REACT_203510. TGF-beta receptor signaling activates SMADs.
    REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    REACT_216222. Transcriptional regulation of pluripotent stem cells.
    REACT_216258. Signaling by Activin.
    REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_220645. Signaling by NODAL.
    REACT_224802. TGFBR1 KD Mutants in Cancer.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mothers against decapentaplegic homolog 2
    Short name:
    MAD homolog 2
    Short name:
    Mothers against DPP homolog 2
    Alternative name(s):
    Mad-related protein 2
    Short name:
    mMad2
    SMAD family member 2
    Short name:
    SMAD 2
    Short name:
    Smad2
    Gene namesi
    Name:Smad2
    Synonyms:Madh2, Madr2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:108051. Smad2.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 By similarity.By similarity

    GO - Cellular componenti

    1. activin responsive factor complex Source: Ensembl
    2. cytoplasm Source: BHF-UCL
    3. nucleus Source: UniProtKB
    4. SMAD protein complex Source: Ensembl
    5. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 467466Mothers against decapentaplegic homolog 2PRO_0000090853Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei8 – 81PhosphothreonineBy similarity
    Modified residuei19 – 191N6-acetyllysineBy similarity
    Modified residuei240 – 2401Phosphoserine; by CAMK2PROSITE-ProRule annotation
    Modified residuei458 – 4581PhosphoserinePROSITE-ProRule annotation
    Modified residuei460 – 4601PhosphoserinePROSITE-ProRule annotation
    Modified residuei464 – 4641PhosphoserinePROSITE-ProRule annotation
    Modified residuei465 – 4651Phosphoserine; by TGFBR1PROSITE-ProRule annotation
    Modified residuei467 – 4671Phosphoserine; by TGFBR1PROSITE-ProRule annotation

    Post-translational modificationi

    In response to TGF-beta, phosphorylated on the C-terminal SXS motif by TGF-beta and activin type 1 receptor kinases, phosphorylation declines progressively in a SETD8-dependent manner. Phosphorylation in this motif is required for interaction with a number of proteins including SMURF2, SNON and SMAD4 in response to TGF-beta. Dephosphorylated in this motif by PPM1A leading to disruption of the SMAD2/3-SMAD4 complex, nuclear export and termination of the TGF-beta signaling. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin. Phosphorylated by PDPK1.2 Publications
    In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation. Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes By similarity.By similarity
    Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ62432.
    PaxDbiQ62432.
    PRIDEiQ62432.

    PTM databases

    PhosphoSiteiQ62432.

    Expressioni

    Gene expression databases

    ArrayExpressiQ62432.
    BgeeiQ62432.
    CleanExiMM_SMAD2.
    GenevestigatoriQ62432.

    Interactioni

    Subunit structurei

    Momomer; the absence of TGF-beta. Interacts with ZNF580. Heterodimer; in the presence of TGF-beta. Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4. Found in a complex with SMAD3 and TRIM33 upon addition of TGF-beta. Interacts with ACVR1B, SMAD3 and TRIM33. Interacts (via the MH2 domain) with ZFYVE9; may form trimers with the SMAD4 co-SMAD. Interacts with FOXH1, homeobox protein TGIF, PEBP2-alpha subunit, CREB-binding protein (CBP), EP300, SKI and SNW1. Interacts with SNON; when phosphorylated at Ser-465/467. Interacts (via PY-motif) with SMURF2. Interacts with SKOR1 and SKOR2. Interacts with PRDM16. Interacts (via MH2 domain) with LEMD3. Interacts with RBPMS. Interacts (dephosphorylated form, via the MH1 and MH2 domains) with RANBP3 (via its C-terminal R domain); the interaction results in the export of dephosphorylated SMAD3 out of the nucleus and termination of the TGF-beta signaling. Interacts with NEDD4L in response to TGF-beta. Interacts with WWP1, AIP1 and HGS. Interacts with PML. Interacts with PDPK1 (via PH domain). Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation. Interacts with USP15. Interacts with PPP5C. Interacts with LDLRAD4 (via the SMAD interaction motif). Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif).6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Smad4P974713EBI-2337932,EBI-5259270

    Protein-protein interaction databases

    BioGridi201275. 35 interactions.
    IntActiQ62432. 4 interactions.
    MINTiMINT-99148.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62432.
    SMRiQ62432. Positions 7-172, 265-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 176167MH1PROSITE-ProRule annotationAdd
    BLAST
    Domaini274 – 467194MH2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi221 – 2255PY-motifBy similarity

    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

    eggNOGiNOG320700.
    GeneTreeiENSGT00600000084186.
    HOGENOMiHOG000286018.
    HOVERGENiHBG053353.
    InParanoidiQ62432.
    KOiK04500.
    OMAiMNQSMDT.
    OrthoDBiEOG7W1540.
    PhylomeDBiQ62432.
    TreeFamiTF314923.

    Family and domain databases

    Gene3Di2.60.200.10. 1 hit.
    3.90.520.10. 1 hit.
    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 (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: mRNA corresponding to the isoform Long is approximately 20-fold more abundant. Both forms are coexpressed throughout mouse development.

    Isoform Long (identifier: Q62432-1) [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

    MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK    50
    KLKKTGRLDE LEKAITTQNC NTKCVTIPST CSEIWGLSTA NTVDQWDTTG 100
    LYSFSEQTRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELKAIENCE 150
    YAFNLKKDEV CVNPYHYQRV ETPVLPPVLV PRHTEILTEL PPLDDYTHSI 200
    PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS MDTGSPAELS 250
    PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD 300
    GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL 350
    SDSAIFVQSP NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ 400
    GFEAVYQLTR MCTIRMSFVK GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD 450
    KVLTQMGSPS VRCSSMS 467
    Length:467
    Mass (Da):52,266
    Last modified:November 14, 2006 - v2
    Checksum:i31A2A36D463DB3E9
    GO
    Isoform Short (identifier: Q62432-2) [UniParc]FASTAAdd to Basket

    Also known as: Deltaexon3

    The sequence of this isoform differs from the canonical sequence as follows:
         79-108: Missing.

    Show »
    Length:437
    Mass (Da):48,956
    Checksum:i0E2FF38B009D2F9E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421E → Q in AAB03612. (PubMed:8756346)Curated
    Sequence conflicti42 – 421E → Q in AAB62269. (PubMed:9328171)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei79 – 10830Missing in isoform Short. 1 PublicationVSP_021571Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U60530 mRNA. Translation: AAB03612.1.
    AF005743 mRNA. Translation: AAB62269.1.
    AK007817 mRNA. Translation: BAB25282.1.
    AY334552 mRNA. Translation: AAR00933.1.
    BC021342 mRNA. Translation: AAH21342.1.
    BC089184 mRNA. Translation: AAH89184.1.
    CCDSiCCDS29350.1. [Q62432-1]
    RefSeqiNP_001239410.1. NM_001252481.1. [Q62432-1]
    NP_034884.2. NM_010754.5. [Q62432-1]
    XP_006525762.1. XM_006525699.1. [Q62432-1]
    XP_006525763.1. XM_006525700.1. [Q62432-2]
    UniGeneiMm.152699.
    Mm.490934.

    Genome annotation databases

    EnsembliENSMUST00000025453; ENSMUSP00000025453; ENSMUSG00000024563. [Q62432-1]
    ENSMUST00000091831; ENSMUSP00000089439; ENSMUSG00000024563. [Q62432-2]
    ENSMUST00000168423; ENSMUSP00000130115; ENSMUSG00000024563. [Q62432-1]
    GeneIDi17126.
    KEGGimmu:17126.
    UCSCiuc008fqn.2. mouse. [Q62432-1]
    uc008fqo.2. mouse. [Q62432-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U60530 mRNA. Translation: AAB03612.1 .
    AF005743 mRNA. Translation: AAB62269.1 .
    AK007817 mRNA. Translation: BAB25282.1 .
    AY334552 mRNA. Translation: AAR00933.1 .
    BC021342 mRNA. Translation: AAH21342.1 .
    BC089184 mRNA. Translation: AAH89184.1 .
    CCDSi CCDS29350.1. [Q62432-1 ]
    RefSeqi NP_001239410.1. NM_001252481.1. [Q62432-1 ]
    NP_034884.2. NM_010754.5. [Q62432-1 ]
    XP_006525762.1. XM_006525699.1. [Q62432-1 ]
    XP_006525763.1. XM_006525700.1. [Q62432-2 ]
    UniGenei Mm.152699.
    Mm.490934.

    3D structure databases

    ProteinModelPortali Q62432.
    SMRi Q62432. Positions 7-172, 265-467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201275. 35 interactions.
    IntActi Q62432. 4 interactions.
    MINTi MINT-99148.

    PTM databases

    PhosphoSitei Q62432.

    Proteomic databases

    MaxQBi Q62432.
    PaxDbi Q62432.
    PRIDEi Q62432.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025453 ; ENSMUSP00000025453 ; ENSMUSG00000024563 . [Q62432-1 ]
    ENSMUST00000091831 ; ENSMUSP00000089439 ; ENSMUSG00000024563 . [Q62432-2 ]
    ENSMUST00000168423 ; ENSMUSP00000130115 ; ENSMUSG00000024563 . [Q62432-1 ]
    GeneIDi 17126.
    KEGGi mmu:17126.
    UCSCi uc008fqn.2. mouse. [Q62432-1 ]
    uc008fqo.2. mouse. [Q62432-2 ]

    Organism-specific databases

    CTDi 4087.
    MGIi MGI:108051. Smad2.

    Phylogenomic databases

    eggNOGi NOG320700.
    GeneTreei ENSGT00600000084186.
    HOGENOMi HOG000286018.
    HOVERGENi HBG053353.
    InParanoidi Q62432.
    KOi K04500.
    OMAi MNQSMDT.
    OrthoDBi EOG7W1540.
    PhylomeDBi Q62432.
    TreeFami TF314923.

    Enzyme and pathway databases

    Reactomei REACT_202264. SMAD4 MH2 Domain Mutants in Cancer.
    REACT_203510. TGF-beta receptor signaling activates SMADs.
    REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    REACT_216222. Transcriptional regulation of pluripotent stem cells.
    REACT_216258. Signaling by Activin.
    REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_220645. Signaling by NODAL.
    REACT_224802. TGFBR1 KD Mutants in Cancer.

    Miscellaneous databases

    NextBioi 291308.
    PROi Q62432.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62432.
    Bgeei Q62432.
    CleanExi MM_SMAD2.
    Genevestigatori Q62432.

    Family and domain databases

    Gene3Di 2.60.200.10. 1 hit.
    3.90.520.10. 1 hit.
    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

    1. "A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway."
      Baker J.C., Harland R.M.
      Genes Dev. 10:1880-1889(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Strain: 129/Sv.
    2. "Smad4 (homolog of human DPC4) and Smad2 (homolog of human JV18-1): candidates for murine lung tumor resistance and suppressor genes."
      Devereux T.R., Anna C.H., Patel A.C., White C.M., Festing M.F., You M.
      Carcinogenesis 18:1751-1755(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Strain: A/J and BALB/c.
    3. "Both SMAD2 and SMAD3 mediate activin-stimulated expression of the follicle-stimulating hormone beta subunit in mouse gonadotrope cells."
      Bernard D.J.
      Mol. Endocrinol. 18:606-623(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Strain: C57BL/6J.
      Tissue: Pancreas.
    5. "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 LONG).
    6. "Functions of mammalian Smad genes as revealed by targeted gene disruption in mice."
      Weinstein M., Yang X., Deng C.-X.
      Cytokine Growth Factor Rev. 11:49-58(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    7. "Cytoplasmic PML function in TGF-beta signalling."
      Lin H.K., Bergmann S., Pandolfi P.P.
      Nature 431:205-211(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH PML AND ZFYVE9/SARA.
    8. "Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1)."
      Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K., Miyazawa K.
      Oncogene 23:6914-6923(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WWP1.
    9. "Mice exclusively expressing the short isoform of Smad2 develop normally and are viable and fertile."
      Dunn N.R., Koonce C.H., Anderson D.C., Islam A., Bikoff E.K., Robertson E.J.
      Genes Dev. 19:152-163(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM SHORT).
    10. "Transforming growth factor-beta 1 inhibits non-pathogenic Gram negative bacteria-induced NF-kappa B recruitment to the interleukin-6 gene promoter in intestinal epithelial cells through modulation of histone acetylation."
      Haller D., Holt L., Kim S.C., Schwabe R.F., Sartor R.B., Jobin C.
      J. Biol. Chem. 278:23851-23860(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
    11. "Identification and characterization of a PDZ protein that interacts with activin types II receptors."
      Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z., Nakamura T., Sugino H.
      J. Biol. Chem. 275:5485-5492(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AIP1.
    12. "Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through cooperation with SARA."
      Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y., Hanai J., Beppu H., Tsukazaki T., Wrana J.L., Miyazono K., Sugamura K.
      Mol. Cell. Biol. 20:9346-9355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HGS.
    13. "NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor."
      Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K., Imamura T.
      Biochem. J. 386:461-470(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEDD4L, UBIQUITINATION.
    14. "Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
      Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
      Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP5C, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSMAD2_MOUSE
    AccessioniPrimary (citable) accession number: Q62432
    Secondary accession number(s): Q6GU18, Q6VP00, Q9D8P6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 14, 2006
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3