Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P97471

- SMAD4_MOUSE

UniProt

P97471 - SMAD4_MOUSE

Protein

Mothers against decapentaplegic homolog 4

Gene

Smad4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for syngernistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator By similarity. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (PubMed:15329343). In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi71 – 711ZincBy similarity
    Metal bindingi115 – 1151ZincBy similarity
    Metal bindingi127 – 1271ZincBy similarity
    Metal bindingi132 – 1321ZincBy similarity
    Sitei514 – 5141Necessary for heterotrimerizationBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. collagen binding Source: MGI
    3. core promoter proximal region sequence-specific DNA binding Source: Ensembl
    4. DNA binding Source: MGI
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: IntAct
    7. RNA polymerase II transcription factor binding Source: BHF-UCL
    8. RNA polymerase II transcription factor binding transcription factor activity Source: BHF-UCL
    9. sequence-specific DNA binding transcription factor activity Source: MGI
    10. transforming growth factor beta receptor, common-partner cytoplasmic mediator activity Source: Ensembl

    GO - Biological processi

    1. anterior/posterior pattern specification Source: MGI
    2. atrioventricular canal development Source: BHF-UCL
    3. atrioventricular valve formation Source: BHF-UCL
    4. axon guidance Source: MGI
    5. BMP signaling pathway Source: Ensembl
    6. brainstem development Source: MGI
    7. branching involved in ureteric bud morphogenesis Source: MGI
    8. cardiac septum development Source: BHF-UCL
    9. cell proliferation Source: MGI
    10. developmental growth Source: MGI
    11. endocardial cell differentiation Source: BHF-UCL
    12. endoderm development Source: MGI
    13. endothelial cell activation Source: BHF-UCL
    14. epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
    15. formation of anatomical boundary Source: MGI
    16. gastrulation Source: MGI
    17. gastrulation with mouth forming second Source: MGI
    18. in utero embryonic development Source: MGI
    19. kidney development Source: MGI
    20. mesoderm development Source: MGI
    21. metanephric mesenchyme morphogenesis Source: UniProtKB
    22. negative regulation of cell death Source: UniProtKB
    23. negative regulation of cell growth Source: Ensembl
    24. negative regulation of cell proliferation Source: MGI
    25. negative regulation of protein catabolic process Source: Ensembl
    26. negative regulation of transcription, DNA-templated Source: Ensembl
    27. nephrogenic mesenchyme morphogenesis Source: UniProtKB
    28. neural crest cell differentiation Source: MGI
    29. neuron fate commitment Source: MGI
    30. palate development Source: BHF-UCL
    31. positive regulation of BMP signaling pathway Source: Ensembl
    32. positive regulation of cell proliferation involved in heart valve morphogenesis Source: BHF-UCL
    33. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
    34. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    35. positive regulation of SMAD protein import into nucleus Source: BHF-UCL
    36. positive regulation of transcription, DNA-templated Source: MGI
    37. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    38. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    39. regulation of binding Source: MGI
    40. regulation of cell proliferation Source: MGI
    41. regulation of hair follicle development Source: MGI
    42. regulation of transcription from RNA polymerase II promoter Source: MGI
    43. regulation of transforming growth factor beta2 production Source: Ensembl
    44. response to hypoxia Source: Ensembl
    45. sebaceous gland development Source: MGI
    46. SMAD protein complex assembly Source: Ensembl
    47. SMAD protein signal transduction Source: Ensembl
    48. somite rostral/caudal axis specification Source: MGI
    49. tissue morphogenesis Source: MGI
    50. transcription from RNA polymerase II promoter Source: GOC
    51. transforming growth factor beta receptor signaling pathway Source: MGI

    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_216222. Transcriptional regulation of pluripotent stem cells.
    REACT_216258. Signaling by Activin.
    REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_220505. Signaling by BMP.
    REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_220645. Signaling by NODAL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mothers against decapentaplegic homolog 4
    Short name:
    MAD homolog 4
    Short name:
    Mothers against DPP homolog 4
    Alternative name(s):
    Deletion target in pancreatic carcinoma 4 homolog
    SMAD family member 4
    Short name:
    SMAD 4
    Short name:
    Smad4
    Gene namesi
    Name:Smad4
    Synonyms:Dpc4, Madh4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:894293. Smad4.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with R-SMAD. PDPK1 prevents its nuclear translocation By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Conditional knockout in muscle leads to muscle atrophy and weakness. Mutant mice loose significantly more muscle mass after denervation as compared to wild-type animals and show excessive proteolysis in denervated muscle. The loss of maximal absolute force after fasting is greater in mutant mice than in controls.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 551551Mothers against decapentaplegic homolog 4PRO_0000090862Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371N6-acetyllysineBy similarity
    Modified residuei427 – 4271N6-acetyllysineBy similarity
    Modified residuei506 – 5061N6-acetyllysineBy similarity
    Cross-linki518 – 518Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Phosphorylated by PDPK1.By similarity
    Monoubiquitinated on Lys-518 by E3 ubiquitin-protein ligase TRIM33. Monoubiquitination hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade. Deubiqitination by USP9X restores its competence to mediate TGF-beta signaling By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP97471.
    PaxDbiP97471.
    PRIDEiP97471.

    PTM databases

    PhosphoSiteiP97471.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP97471.
    BgeeiP97471.
    CleanExiMM_SMAD4.
    GenevestigatoriP97471.

    Interactioni

    Subunit structurei

    Monomer By similarity. Heterotrimer; with a C-terminally phosphorylated R-SMAD molecule and to form the transcriptionally active SMAD2/3-SMAD4 complex By similarity. Found in a ternary complex composed of SMAD4, STK11/LKB1 and STK11IP. Interacts with ATF2, COPS5, DACH1, MSG1, SKI, STK11/LKB1, STK11IP and TRIM33. Associates with ZNF423 or ZNF521 in response to BMP2 leading to activate transcription of BMP target genes. Interacts with USP9X. Interacts with RBPMS. Interacts with WWTR1 (via coiled-coil domain). Interacts with CITED1 and CITED2 By similarity. Interacts with PDPK1 (via PH domain) By similarity. Interacts with VPS39; this interaction affects heterodimer formation with SMAD3, but not with SMAD2, and leads to inhibition of SMAD3-dependent transcription activation By similarity. Interactions with VPS39 and SMAD2 may be mutually exclusive By similarity. Found in a complex with SMAD1 and YY1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Smad2Q624323EBI-5259270,EBI-2337932
    Smad3Q8BUN55EBI-5259270,EBI-2337983

    Protein-protein interaction databases

    BioGridi201277. 27 interactions.
    DIPiDIP-29718N.
    IntActiP97471. 5 interactions.
    MINTiMINT-261841.

    Structurei

    Secondary structure

    1
    551
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 249
    Helixi33 – 4715
    Helixi51 – 6212
    Turni63 – 653
    Beta strandi73 – 753
    Beta strandi82 – 843
    Beta strandi87 – 893
    Helixi91 – 999
    Beta strandi109 – 1113
    Helixi119 – 1213
    Beta strandi124 – 1274
    Helixi130 – 1323
    Beta strandi133 – 1353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QSVX-ray2.71A/B/C/D9-140[»]
    ProteinModelPortaliP97471.
    SMRiP97471. Positions 10-138, 284-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP97471.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 142125MH1PROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 551230MH2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 31946SADAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi450 – 46516Poly-AlaAdd
    BLAST

    Domaini

    The MH1 domain is required for DNA binding.
    The MH2 domain is required for both homomeric and heteromeric interactions and for transcriptional regulation. Sufficient for nuclear import By similarity.By 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

    eggNOGiNOG286923.
    GeneTreeiENSGT00600000084353.
    HOGENOMiHOG000286019.
    HOVERGENiHBG053353.
    InParanoidiQ6GTP6.
    KOiK04501.
    OMAiPTEGHSI.
    OrthoDBiEOG712TW5.
    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. 1 hit.
    PROSITEiPS51075. MH1. 1 hit.
    PS51076. MH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P97471-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK    50
    KDELDSLITA ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR 100
    WPDLHKNELK HVKYCQYAFD LKCDSVCVNP YHYERVVSPG IDLSGLTLQS 150
    NAPSMLVKDE YVHDFEGQPS LPTEGHSIQT IQHPPSNRAS TETYSAPALL 200
    APAESNATST TNFPNIPVAS TSQPASILAG SHSEGLLQIA SGPQPGQQQN 250
    GFTAQPATYH HNSTTTWTGS RTAPYTPNLP HHQNGHLQHH PPMPPHPGHY 300
    WPVHNELAFQ PPISNHPAPE YWCSIAYFEM DVQVGETFKV PSSCPVVTVD 350
    GYVDPSGGDR FCLGQLSNVH RTEAIERARL HIGKGVQLEC KGEGDVWVRC 400
    LSDHAVFVQS YYLDREAGRA PGDAVHKIYP SAYIKVFDLR QCHRQMQQQA 450
    ATAQAAAAAQ AAAVAGNIPG PGSVGGIAPA ISLSAAAGIG VDDLRRLCIL 500
    RMSFVKGWGP DYPRQSIKET PCWIEIHLHR ALQLLDEVLH TMPIADPQPL 550
    D 551
    Length:551
    Mass (Da):60,342
    Last modified:July 27, 2011 - v2
    Checksum:i4FBDF5DED4442F86
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti257 – 2571A → S in AAB57905. (PubMed:9166592)Curated
    Sequence conflicti292 – 2921P → R in AAB57905. (PubMed:9166592)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U79748 mRNA. Translation: AAB57905.1.
    CH466528 Genomic DNA. Translation: EDL09560.1.
    BC046584 mRNA. Translation: AAH46584.1.
    AK004804 mRNA. Translation: BAB23576.1.
    CCDSiCCDS29337.1.
    RefSeqiNP_032566.2. NM_008540.2.
    UniGeneiMm.100399.

    Genome annotation databases

    EnsembliENSMUST00000025393; ENSMUSP00000025393; ENSMUSG00000024515.
    ENSMUST00000114939; ENSMUSP00000110589; ENSMUSG00000024515.
    GeneIDi17128.
    KEGGimmu:17128.
    UCSCiuc008fou.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U79748 mRNA. Translation: AAB57905.1 .
    CH466528 Genomic DNA. Translation: EDL09560.1 .
    BC046584 mRNA. Translation: AAH46584.1 .
    AK004804 mRNA. Translation: BAB23576.1 .
    CCDSi CCDS29337.1.
    RefSeqi NP_032566.2. NM_008540.2.
    UniGenei Mm.100399.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QSV X-ray 2.71 A/B/C/D 9-140 [» ]
    ProteinModelPortali P97471.
    SMRi P97471. Positions 10-138, 284-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201277. 27 interactions.
    DIPi DIP-29718N.
    IntActi P97471. 5 interactions.
    MINTi MINT-261841.

    PTM databases

    PhosphoSitei P97471.

    Proteomic databases

    MaxQBi P97471.
    PaxDbi P97471.
    PRIDEi P97471.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025393 ; ENSMUSP00000025393 ; ENSMUSG00000024515 .
    ENSMUST00000114939 ; ENSMUSP00000110589 ; ENSMUSG00000024515 .
    GeneIDi 17128.
    KEGGi mmu:17128.
    UCSCi uc008fou.1. mouse.

    Organism-specific databases

    CTDi 4089.
    MGIi MGI:894293. Smad4.

    Phylogenomic databases

    eggNOGi NOG286923.
    GeneTreei ENSGT00600000084353.
    HOGENOMi HOG000286019.
    HOVERGENi HBG053353.
    InParanoidi Q6GTP6.
    KOi K04501.
    OMAi PTEGHSI.
    OrthoDBi EOG712TW5.
    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_216222. Transcriptional regulation of pluripotent stem cells.
    REACT_216258. Signaling by Activin.
    REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_220505. Signaling by BMP.
    REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_220645. Signaling by NODAL.

    Miscellaneous databases

    EvolutionaryTracei P97471.
    NextBioi 291316.
    PROi P97471.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97471.
    Bgeei P97471.
    CleanExi MM_SMAD4.
    Genevestigatori P97471.

    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. 1 hit.
    PROSITEi PS51075. MH1. 1 hit.
    PS51076. MH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and chromosomal mapping of the mouse homolog (Madh4) of the human DPC4/MADH4 gene."
      Anna C.H., Devereux T.R.
      Mamm. Genome 8:443-444(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: A/J.
      Tissue: Lung.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Olfactory epithelium.
    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] OF 67-551.
      Strain: C57BL/6J.
      Tissue: Lung.
    5. "SMAD-mediated modulation of YY1 activity regulates the BMP response and cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5 enhancer."
      Lee K.H., Evans S., Ruan T.Y., Lassar A.B.
      Development 131:4709-4723(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH SMAD1 AND YY1.
    6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements of BMP and TGF-beta effectors."
      Baburajendran N., Palasingam P., Narasimhan K., Sun W., Prabhakar S., Jauch R., Kolatkar P.R.
      Nucleic Acids Res. 38:3477-3488(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 9-140 IN COMPLEX WITH DNA, ZINC_BINDING SITES, SUBUNIT.

    Entry informationi

    Entry nameiSMAD4_MOUSE
    AccessioniPrimary (citable) accession number: P97471
    Secondary accession number(s): Q6GTP6, Q9CW56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 141 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

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3