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P70340

- SMAD1_MOUSE

UniProt

P70340 - SMAD1_MOUSE

Protein

Mothers against decapentaplegic homolog 1

Gene

Smad1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD) By similarity. May play a role in the initiation and maintenance of spermatogenesis. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 By similarity. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343).By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Zinc
    Metal bindingi109 – 1091Zinc
    Metal bindingi121 – 1211Zinc
    Metal bindingi126 – 1261Zinc

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
    4. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. BMP signaling pathway Source: UniProtKB
    2. bone development Source: MGI
    3. cardiac muscle cell proliferation Source: MGI
    4. cartilage development Source: MGI
    5. cellular response to BMP stimulus Source: BHF-UCL
    6. cellular response to organic cyclic compound Source: MGI
    7. embryonic pattern specification Source: UniProtKB
    8. gamete generation Source: MGI
    9. hindbrain development Source: MGI
    10. homeostatic process Source: MGI
    11. inflammatory response Source: UniProtKB
    12. kidney development Source: Ensembl
    13. MAPK cascade Source: MGI
    14. mesodermal cell fate commitment Source: MGI
    15. midbrain development Source: MGI
    16. negative regulation of cell proliferation Source: MGI
    17. negative regulation of muscle cell apoptotic process Source: Ensembl
    18. osteoblast fate commitment Source: MGI
    19. positive regulation of cartilage development Source: MGI
    20. positive regulation of dendrite morphogenesis Source: Ensembl
    21. positive regulation of gene expression Source: MGI
    22. positive regulation of osteoblast differentiation Source: MGI
    23. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    24. positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: BHF-UCL
    25. protein phosphorylation Source: MGI
    26. regulation of transcription from RNA polymerase II promoter Source: MGI
    27. response to drug Source: Ensembl
    28. response to organonitrogen compound Source: Ensembl
    29. SMAD protein complex assembly Source: Ensembl
    30. transcription, DNA-templated Source: UniProtKB-KW
    31. transforming growth factor beta receptor signaling pathway Source: InterPro
    32. ureteric bud development Source: UniProtKB
    33. wound healing Source: Ensembl

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_220505. Signaling by BMP.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mothers against decapentaplegic homolog 1
    Short name:
    MAD homolog 1
    Short name:
    Mothers against DPP homolog 1
    Alternative name(s):
    Dwarfin-A
    Short name:
    Dwf-A
    Mothers-against-DPP-related 1
    Short name:
    Mad-related protein 1
    Short name:
    mMad1
    SMAD family member 1
    Short name:
    SMAD 1
    Short name:
    Smad1
    Gene namesi
    Name:Smad1
    Synonyms:Madh1, Madr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:109452. Smad1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4. Colocalizes with LEMD3 at the nucleus inner membrane By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear inner membrane Source: Ensembl
    3. nucleus Source: UniProtKB
    4. protein complex Source: MGI
    5. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Mothers against decapentaplegic homolog 1PRO_0000090848Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei322 – 3221Phosphothreonine; by MINK1, TNIK and MAP4K4
    Modified residuei463 – 4631PhosphoserinePROSITE-ProRule annotation
    Modified residuei465 – 4651PhosphoserinePROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated on serine by BMP type 1 receptor kinase.By similarity
    Ubiquitinated by SMAD-specific E3 ubiquitin ligase SMURF1, leading to 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

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP70340.
    PaxDbiP70340.
    PRIDEiP70340.

    PTM databases

    PhosphoSiteiP70340.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Developmental stagei

    Ubiquitously expressed during embryogenesis. Expression starts in some seminiferous tubules at 2 weeks of age. After mid-puberty a stage-specific expression is established. During the cycling of the seminiferous epithelium, expression initiates in the pachytene spermatocytes of stage V seminiferous tubules, peaks at stage X, then decreases as pachytene spermatocytes differentiate into secondary spermatocytes and then round spermatids.

    Gene expression databases

    ArrayExpressiP70340.
    BgeeiP70340.
    CleanExiMM_SMAD1.
    GenevestigatoriP70340.

    Interactioni

    Subunit structurei

    May form trimers with another SMAD1 and the co-SMAD SMAD4. Interacts with PEBP2-alpha subunit, CREB-binding protein (CBP), p300, SMURF1, SMURF2, USP15 and HOXC8. Associates with ZNF423 or ZNF521 in response to BMP2 leading to activate transcription of BMP target genes. Interacts with SKOR1. Interacts (via MH2 domain) with LEMD3. Binding to LEMD3 results in at least a partial reduction of receptor-mediated phosphorylation By similarity. Also interacts with HGS, NANOG and ZCCHC12. Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into the 20S proteasome By similarity. Found in a complex with SMAD4 and YY1.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Map3k7Q620733EBI-6992047,EBI-1775345

    Protein-protein interaction databases

    BioGridi201274. 34 interactions.
    IntActiP70340. 7 interactions.
    MINTiMINT-99213.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 198
    Helixi25 – 4117
    Helixi47 – 5610
    Beta strandi66 – 683
    Beta strandi71 – 733
    Beta strandi75 – 773
    Beta strandi80 – 823
    Helixi84 – 929
    Helixi100 – 1023
    Beta strandi103 – 1053
    Helixi113 – 1153
    Beta strandi118 – 1214
    Helixi124 – 1263
    Beta strandi127 – 1293

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KMPX-ray2.70A/B9-132[»]
    ProteinModelPortaliP70340.
    SMRiP70340. Positions 9-132, 268-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP70340.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 136125MH1PROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 465195MH2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 457Poly-Lys

    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

    eggNOGiNOG330956.
    GeneTreeiENSGT00600000084186.
    HOGENOMiHOG000286018.
    HOVERGENiHBG053353.
    InParanoidiQ6GT95.
    KOiK04676.
    OMAiPRNSEFN.
    OrthoDBiEOG7W1540.
    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.

    P70340-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE    50
    LEKALSCPGQ PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH 100
    HELKPLECCE FPFGSKQKEV CINPYHYKRV ESPVLPPVLV PRHSEYNPQH 150
    SLLAQFRNLG QNEPHMPLNA TFPDSFQQPN SHPFPHSPNS SYPNSPGGSS 200
    STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMAQDGSQ PMDTNMMAPP 250
    LPAEISRGDV QAVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT 300
    DPSNNKNRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD 350
    SSIFVQSRNC NYHHGFHPTT VCKIPSGCSL KIFNNQEFAQ LLAQSVNHGF 400
    ETVYELTKMC TIRMSFVKGW GAEYHRQDVT STPCWIEIHL HGPLQWLDKV 450
    LTQMGSPHNP ISSVS 465
    Length:465
    Mass (Da):52,157
    Last modified:July 27, 2011 - v2
    Checksum:i07A56FBEE79A1C2A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951P → S in AAC52785. (PubMed:8799132)Curated
    Sequence conflicti95 – 951P → S in AAG41407. (PubMed:11111041)Curated
    Sequence conflicti142 – 1421R → K in AAC52785. (PubMed:8799132)Curated
    Sequence conflicti142 – 1421R → K in AAG41407. (PubMed:11111041)Curated
    Sequence conflicti199 – 2002SS → QG in AAB18256. (PubMed:9076678)Curated
    Sequence conflicti393 – 3931A → E in AAB18256. (PubMed:9076678)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58992 mRNA. Translation: AAC52785.1.
    U74359 mRNA. Translation: AAB18256.1.
    AF295768
    , AF295763, AF295764, AF295765, AF295766, AF295767 Genomic DNA. Translation: AAG41407.1.
    AK017583 mRNA. Translation: BAB30820.1.
    AK054104 mRNA. Translation: BAC35658.1.
    BC058693 mRNA. Translation: AAH58693.1.
    CCDSiCCDS22437.1.
    RefSeqiNP_032565.2. NM_008539.3.
    XP_006530809.1. XM_006530746.1.
    UniGeneiMm.223717.

    Genome annotation databases

    EnsembliENSMUST00000066091; ENSMUSP00000071035; ENSMUSG00000031681.
    GeneIDi17125.
    KEGGimmu:17125.
    UCSCiuc009mip.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58992 mRNA. Translation: AAC52785.1 .
    U74359 mRNA. Translation: AAB18256.1 .
    AF295768
    , AF295763 , AF295764 , AF295765 , AF295766 , AF295767 Genomic DNA. Translation: AAG41407.1 .
    AK017583 mRNA. Translation: BAB30820.1 .
    AK054104 mRNA. Translation: BAC35658.1 .
    BC058693 mRNA. Translation: AAH58693.1 .
    CCDSi CCDS22437.1.
    RefSeqi NP_032565.2. NM_008539.3.
    XP_006530809.1. XM_006530746.1.
    UniGenei Mm.223717.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KMP X-ray 2.70 A/B 9-132 [» ]
    ProteinModelPortali P70340.
    SMRi P70340. Positions 9-132, 268-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201274. 34 interactions.
    IntActi P70340. 7 interactions.
    MINTi MINT-99213.

    PTM databases

    PhosphoSitei P70340.

    Proteomic databases

    MaxQBi P70340.
    PaxDbi P70340.
    PRIDEi P70340.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000066091 ; ENSMUSP00000071035 ; ENSMUSG00000031681 .
    GeneIDi 17125.
    KEGGi mmu:17125.
    UCSCi uc009mip.2. mouse.

    Organism-specific databases

    CTDi 4086.
    MGIi MGI:109452. Smad1.

    Phylogenomic databases

    eggNOGi NOG330956.
    GeneTreei ENSGT00600000084186.
    HOGENOMi HOG000286018.
    HOVERGENi HBG053353.
    InParanoidi Q6GT95.
    KOi K04676.
    OMAi PRNSEFN.
    OrthoDBi EOG7W1540.
    TreeFami TF314923.

    Enzyme and pathway databases

    Reactomei REACT_220505. Signaling by BMP.

    Miscellaneous databases

    ChiTaRSi SMAD1. mouse.
    EvolutionaryTracei P70340.
    NextBioi 291304.
    PROi P70340.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70340.
    Bgeei P70340.
    CleanExi MM_SMAD1.
    Genevestigatori P70340.

    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. "Mammalian dwarfins are phosphorylated in response to transforming growth factor beta and are implicated in control of cell growth."
      Yingling J.M., Das P., Savage C., Zhang M., Padgett R.W., Wang X.-F.
      Proc. Natl. Acad. Sci. U.S.A. 93:8940-8944(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryo.
    2. "Evidence that Mothers-against-dpp-related 1 (Madr1) plays a role in the initiation and maintenance of spermatogenesis in the mouse."
      Zhao G.-Q., Hogan B.L.M.
      Mech. Dev. 61:63-73(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryonic heart.
    3. "Characterization of the mouse Smad1 gene and its expression pattern in adult mouse tissues."
      Huang S., Flanders K.C., Roberts A.B.
      Gene 258:43-53(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    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].
      Strain: C57BL/6J.
      Tissue: Embryo and Oviduct.
    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].
      Strain: C57BL/6.
      Tissue: Brain.
    6. "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.
    7. "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, IDENTIFICATION IN A COMPLEX WITH SMAD4 AND YY1.
    8. "Nanog binds to Smad1 and blocks bone morphogenetic protein-induced differentiation of embryonic stem cells."
      Suzuki A., Raya A., Kawakami Y., Morita M., Matsui T., Nakashima K., Gage F.H., Rodriguez-Esteban C., Izpisua Belmonte J.C.
      Proc. Natl. Acad. Sci. U.S.A. 103:10294-10299(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NANOG.
    9. "Sizn1 is a novel protein that functions as a transcriptional coactivator of bone morphogenic protein signaling."
      Cho G., Lim Y., Zand D., Golden J.A.
      Mol. Cell. Biol. 28:1565-1572(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZCCHC12.
    10. "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 (2.7 ANGSTROMS) OF 9-132 IN COMPLEX WITH DNA, ZINC_BINDING SITES, SUBUNIT.

    Entry informationi

    Entry nameiSMAD1_MOUSE
    AccessioniPrimary (citable) accession number: P70340
    Secondary accession number(s): P70442, Q6GT95, Q9CYK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 146 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