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Q15797

- SMAD1_HUMAN

UniProt

Q15797 - SMAD1_HUMAN

Protein

Mothers against decapentaplegic homolog 1

Gene

SMAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression.1 Publication

    Sites

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

    GO - Molecular functioni

    1. co-SMAD binding Source: BHF-UCL
    2. identical protein binding Source: BHF-UCL
    3. I-SMAD binding Source: BHF-UCL
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. receptor signaling protein activity Source: UniProtKB
    8. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
    9. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    10. transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Source: BHF-UCL

    GO - Biological processi

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

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_12034. Signaling by BMP.
    SignaLinkiQ15797.

    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):
    JV4-1
    Mad-related protein 1
    SMAD family member 1
    Short name:
    SMAD 1
    Short name:
    Smad1
    Short name:
    hSMAD1
    Transforming growth factor-beta-signaling protein 1
    Short name:
    BSP-1
    Gene namesi
    Name:SMAD1
    Synonyms:BSP1, MADH1, MADR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:6767. SMAD1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. Co-localizes with LEMD3 at the nucleus inner membrane.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. integral component of membrane Source: UniProtKB
    4. intracellular Source: UniProtKB
    5. mitochondrion Source: HPA
    6. nuclear inner membrane Source: UniProtKB
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProtKB
    9. protein complex Source: MGI
    10. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    SMAD1 variants may be associated with susceptibility to pulmonary hypertension, a disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi419 – 4191G → S: Loss of phosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA30524.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Mothers against decapentaplegic homolog 1PRO_0000090847Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei322 – 3221Phosphothreonine; by MINK1, TNIK and MAP4K41 Publication
    Modified residuei463 – 4631Phosphoserine1 PublicationPROSITE-ProRule annotation
    Modified residuei465 – 4651Phosphoserine1 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated on serine by BMP type 1 receptor kinase.2 Publications
    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.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15797.
    PaxDbiQ15797.
    PRIDEiQ15797.

    PTM databases

    PhosphoSiteiQ15797.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest expression seen in the heart and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ15797.
    BgeeiQ15797.
    CleanExiHS_SMAD1.
    GenevestigatoriQ15797.

    Organism-specific databases

    HPAiCAB005389.
    HPA045647.

    Interactioni

    Subunit structurei

    Found in a complex with SMAD4 and YY1. Interacts with HGS, NANOG and ZCCHC12 By similarity. 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. Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into the 20S proteasome.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102756EBI-1567153,EBI-608057
    GSK3BP498412EBI-1567153,EBI-373586
    SMAD4Q134852EBI-1567153,EBI-347263
    SMURF1Q9HCE74EBI-1567153,EBI-976466
    UCHL3P153742EBI-1567153,EBI-954554
    YAP1P469373EBI-1567153,EBI-1044059

    Protein-protein interaction databases

    BioGridi110261. 115 interactions.
    DIPiDIP-38538N.
    IntActiQ15797. 55 interactions.
    MINTiMINT-244113.
    STRINGi9606.ENSP00000305769.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi272 – 2787
    Beta strandi291 – 2999
    Beta strandi305 – 3106
    Helixi321 – 3277
    Beta strandi334 – 3385
    Beta strandi340 – 3478
    Beta strandi349 – 3513
    Beta strandi353 – 3564
    Helixi358 – 3636
    Beta strandi372 – 3743
    Beta strandi379 – 3846
    Helixi385 – 3939
    Turni394 – 3985
    Helixi400 – 4045
    Helixi405 – 4106
    Beta strandi411 – 4177
    Helixi429 – 4313
    Beta strandi432 – 4409
    Helixi441 – 45111
    Beta strandi461 – 4633

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KHUX-ray2.50A/B/C/D248-465[»]
    2LAWNMR-B222-233[»]
    2LAXNMR-B201-209[»]
    2LAYNMR-B201-209[»]
    2LAZNMR-B210-217[»]
    2LB0NMR-B208-217[»]
    2LB1NMR-B221-233[»]
    3Q47X-ray1.70C456-464[»]
    3Q4AX-ray1.54C456-465[»]
    ProteinModelPortaliQ15797.
    SMRiQ15797. Positions 9-132, 268-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15797.

    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
    Compositional biasi198 – 2014Poly-Ser

    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.
    HOGENOMiHOG000286019.
    HOVERGENiHBG053353.
    InParanoidiQ15797.
    KOiK04676.
    OMAiPRNSEFN.
    PhylomeDBiQ15797.
    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.

    Q15797-1 [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 SYPNSPGSSS 200
    STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMTQDGSQ PMDTNMMAPP 250
    LPSEINRGDV 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):52,260
    Last modified:November 1, 1996 - v1
    Checksum:i2DD34B7F434DBC7E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31V → A Found in a patient with primary pulmonary hypertension; unknown pathological significance; affects SMAD-mediated signaling. 1 Publication
    VAR_066869

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59912 mRNA. Translation: AAC50790.1.
    U59423 mRNA. Translation: AAB06852.1.
    U54826 mRNA. Translation: AAC50493.1.
    U57456 mRNA. Translation: AAC50621.1.
    BT007386 mRNA. Translation: AAP36050.1.
    AK293055 mRNA. Translation: BAF85744.1.
    CH471056 Genomic DNA. Translation: EAX05037.1.
    CH471056 Genomic DNA. Translation: EAX05038.1.
    CH471056 Genomic DNA. Translation: EAX05040.1.
    BC001878 mRNA. Translation: AAH01878.1.
    CCDSiCCDS3765.1.
    PIRiS68987.
    RefSeqiNP_001003688.1. NM_001003688.1.
    NP_005891.1. NM_005900.2.
    XP_005263048.1. XM_005262991.1.
    XP_005263049.1. XM_005262992.2.
    XP_006714280.1. XM_006714217.1.
    UniGeneiHs.604588.

    Genome annotation databases

    EnsembliENST00000302085; ENSP00000305769; ENSG00000170365.
    ENST00000394092; ENSP00000377652; ENSG00000170365.
    ENST00000515385; ENSP00000426568; ENSG00000170365.
    GeneIDi4086.
    KEGGihsa:4086.
    UCSCiuc003ikc.3. human.

    Polymorphism databases

    DMDMi13633915.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59912 mRNA. Translation: AAC50790.1 .
    U59423 mRNA. Translation: AAB06852.1 .
    U54826 mRNA. Translation: AAC50493.1 .
    U57456 mRNA. Translation: AAC50621.1 .
    BT007386 mRNA. Translation: AAP36050.1 .
    AK293055 mRNA. Translation: BAF85744.1 .
    CH471056 Genomic DNA. Translation: EAX05037.1 .
    CH471056 Genomic DNA. Translation: EAX05038.1 .
    CH471056 Genomic DNA. Translation: EAX05040.1 .
    BC001878 mRNA. Translation: AAH01878.1 .
    CCDSi CCDS3765.1.
    PIRi S68987.
    RefSeqi NP_001003688.1. NM_001003688.1.
    NP_005891.1. NM_005900.2.
    XP_005263048.1. XM_005262991.1.
    XP_005263049.1. XM_005262992.2.
    XP_006714280.1. XM_006714217.1.
    UniGenei Hs.604588.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KHU X-ray 2.50 A/B/C/D 248-465 [» ]
    2LAW NMR - B 222-233 [» ]
    2LAX NMR - B 201-209 [» ]
    2LAY NMR - B 201-209 [» ]
    2LAZ NMR - B 210-217 [» ]
    2LB0 NMR - B 208-217 [» ]
    2LB1 NMR - B 221-233 [» ]
    3Q47 X-ray 1.70 C 456-464 [» ]
    3Q4A X-ray 1.54 C 456-465 [» ]
    ProteinModelPortali Q15797.
    SMRi Q15797. Positions 9-132, 268-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110261. 115 interactions.
    DIPi DIP-38538N.
    IntActi Q15797. 55 interactions.
    MINTi MINT-244113.
    STRINGi 9606.ENSP00000305769.

    PTM databases

    PhosphoSitei Q15797.

    Polymorphism databases

    DMDMi 13633915.

    Proteomic databases

    MaxQBi Q15797.
    PaxDbi Q15797.
    PRIDEi Q15797.

    Protocols and materials databases

    DNASUi 4086.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302085 ; ENSP00000305769 ; ENSG00000170365 .
    ENST00000394092 ; ENSP00000377652 ; ENSG00000170365 .
    ENST00000515385 ; ENSP00000426568 ; ENSG00000170365 .
    GeneIDi 4086.
    KEGGi hsa:4086.
    UCSCi uc003ikc.3. human.

    Organism-specific databases

    CTDi 4086.
    GeneCardsi GC04P146402.
    HGNCi HGNC:6767. SMAD1.
    HPAi CAB005389.
    HPA045647.
    MIMi 601595. gene.
    neXtProti NX_Q15797.
    PharmGKBi PA30524.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG330956.
    HOGENOMi HOG000286019.
    HOVERGENi HBG053353.
    InParanoidi Q15797.
    KOi K04676.
    OMAi PRNSEFN.
    PhylomeDBi Q15797.
    TreeFami TF314923.

    Enzyme and pathway databases

    Reactomei REACT_12034. Signaling by BMP.
    SignaLinki Q15797.

    Miscellaneous databases

    EvolutionaryTracei Q15797.
    GeneWikii Mothers_against_decapentaplegic_homolog_1.
    GenomeRNAii 4086.
    NextBioi 16014.
    PROi Q15797.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15797.
    Bgeei Q15797.
    CleanExi HS_SMAD1.
    Genevestigatori Q15797.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A human Mad protein acting as a BMP-regulated transcriptional activator."
      Liu F., Hata A., Baker J.C., Doody J., Carcamo J., Harland R.M., Massague J.
      Nature 381:620-623(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    3. "MADR1, a MAD-related protein that functions in BMP2 signaling pathways."
      Hoodless P.A., Haerry T., Abdollah S., Stapleton M., O'Connor M.B., Attisano L., Wrana J.L.
      Cell 85:489-500(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLY-419.
    4. "Serine phosphorylation, chromosomal localization, and transforming growth factor-beta signal transduction by human bsp-1."
      Lechleider R.J., de Caestecker M.P., Dehejia A., Polymeropoulos M.H., Roberts A.B.
      J. Biol. Chem. 271:17617-17620(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary carcinoma.
    5. "Receptor-associated Mad homologues synergize as effectors of the TGF-beta response."
      Zhang Y., Feng X.-H., Wu R.-Y., Derynck R.
      Nature 383:168-172(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "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].
      Tissue: Uterus.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Placenta.
    10. Bienvenut W.V., Lempens A., Norman J.C.
      Submitted (OCT-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-15; 33-39; 129-157; 283-306 AND 309-319, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    11. "The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase."
      Kretzschmar M., Liu F., Hata A., Doody J., Massague J.
      Genes Dev. 11:984-995(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-463 AND SER-465.
    12. Cited for: REVIEW.
    13. "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.
    14. "OAZ uses distinct DNA- and protein-binding zinc fingers in separate BMP-Smad and Olf signaling pathways."
      Hata A., Seoane J., Lagna G., Montalvo E., Hemmati-Brivanlou A., Massague J.
      Cell 100:229-240(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF423.
    15. Cited for: REVIEW.
    16. Cited for: REVIEW.
    17. "A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)."
      Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y., Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.
      BMC Cell Biol. 3:15-15(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH PSMB4 AND OAZ1, FUNCTION.
    18. "Early hematopoietic zinc finger protein (EHZF), the human homolog to mouse Evi3, is highly expressed in primitive human hematopoietic cells."
      Bond H.M., Mesuraca M., Carbone E., Bonelli P., Agosti V., Amodio N., De Rosa G., Di Nicola M., Gianni A.M., Moore M.A., Hata A., Grieco M., Morrone G., Venuta S.
      Blood 103:2062-2070(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF521.
    19. "The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines."
      Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K.
      J. Biol. Chem. 280:15992-16001(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LEMD3.
    20. "Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP signaling."
      Arndt S., Poser I., Moser M., Bosserhoff A.-K.
      Mol. Cell. Neurosci. 34:603-611(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKOR1.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: PHOSPHORYLATION AT THR-322.
    23. Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP15, DNA-BINDING, INTERACTION WITH USP15.
    24. "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: SUBCELLULAR LOCATION.
    25. Cited for: POSSIBLE INVOLVEMENT IN PULMONARY HYPERTENSION, VARIANT ALA-3, CHARACTERIZATION OF VARIANT ALA-3.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSMAD1_HUMAN
    AccessioniPrimary (citable) accession number: Q15797
    Secondary accession number(s): A8KAJ0, D3DNZ9, Q16636
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 165 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, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3