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0SMAD1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSMAD1
DescriptionMothers against decapentaplegic homolog 1 (smad 1) (mothers against dpp homolog 1) (mad-related protein 1) (transforming growth factor- beta signaling protein 1) (bsp-1) (hsmad1) (jv4-1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (NAS)
0005634 nucleus (NAS)
0005057 receptor signaling protein activity (NAS)
0003700 transcription factor activity (ISS)
0016563 transcriptional activator activity (NAS)
0030509 BMP signaling pathway (ISS)
0009880 embryonic pattern specification (ISS)
0006355 regulation of transcription, DNA-dependent (ISS)
0007165 signal transduction (NAS)
0007179 transforming growth factor beta receptor si... (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Mammalian dwarfins are phosphorylated in response to transforming growth factor beta and are implicated in control of cell growth . The dwarfin family also includes the Drosophila protein MAD that is required for the function of decapentaplegic (DPP) and may play a role in DPP signaling. Drosophila Mad binds to DNA and directly mediates activation of vestigial by Dpp . This domain is also found in nuclear factor I (NF-I) or CCAAT box-binding transcription factor (CTF).This entry represents the MH1 (MAD homology 1) domain is found at the amino terminus of MAD related proteins such as Smads. This domain is separated from the MH2 domain by a non-conserved linker region. The crystal structure of the MH1 domain shows that a highly conserved 11 residue beta hairpin is used to bind the DNA consensus sequence GNCN in the major groove.hown to be vital for the transcriptional activation of target genes. Not all examples of MH1 can bind to DNA however. Smad2 cannot bind DNA and has a large insertion within the hairpin that presumably abolishes DNA binding. A basic helix (H2) in MH1 with the nuclear localisation signal KKLKK has been shown to be essential for Smad3 nuclear import. Smads also use the MH1 domain to interact with transcription factors such as Jun.FE3.p1.nd Runx .
  IPR003619:MAD homology 1, Dwarfin-type
Mammalian dwarfins are phosphorylated in response to transforming growth factor beta and are implicated in control of cell growth . The dwarfin family also includes the Drosophila protein MAD that is required for the function of decapentaplegic (DPP) and may play a role in DPP signaling. Drosophila Mad binds to DNA and directly mediates activation of vestigial by Dpp . This domain is also found in nuclear factor I (NF-I) or CCAAT box-binding transcription factor (CTF).This entry represents the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD related proteins such as Smads. This domain is separated from the MH1 domain by a non-conserved linker region. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers. Unlike MH1.H2 does not bind DNA. The well-studied MH2 domain of Smad4 is composed of five alpha helices and three loops enclosing a beta sandwich. Smads are involved in the propagation of TGF-beta signals by direct association with the TGF-beta receptor kinase which phosphorylates the last two Ser of a conserved SSXS motif located at the C-terminus of MH2 .
  IPR001132:MAD homology 2, Dwarfin-type
FHA and SMAD (MH2) domains share a common structure consisting of a sandwich of eleven beta strands in two sheets with Greek key topology. Forkhead-associated (FHA) domains were originally identified as a sequence profile of about 75 amino acids.hereas the full-length domain is closer to about 150 amino acids. FHA domains are found in transcription factors.inesin motors.nd in a variety of other signalling molecules in organisms ranging from eubacteria to humans. FHA domains are protein-protein interaction domains that are specific for phosphoproteins. FHA-containing proteins function in maintaining cell-cycle checkpoints.NA repair and transcriptional regulation. FHA domain proteins include the Chk2/Rad53/Cds1 family of proteins that contain one or more FHA domains.s well as a Ser/Thr kinase domain . SMAD domain proteins are found in a range of species from nematodes to humans. These highly conserved proteins contain an N-terminal MH1 domain that contacts DNA.nd is separated by a short linker region from the C-terminal MH2 domain.he later showing a striking similarity to FHA domains. SMAD proteins mediate signalling by the TGF-beta/activin/BMP-2/4 cytokines from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD proteins fall into three functional classes: the receptor-regulated SMADs (R-SMADs).ncluding SMAD1.2.3.5.nd -8.ach of which is involved in a ligand-specific signalling pathway ; the comediator SMADs (co-SMADs).ncluding SMAD4.hich interact with R-SMADs to participate in signalling ; and the inhibitory SMADs (I-SMADs).ncluding SMAD6 and -7.hich block the activation of R-SMADs and Co-SMADs.hereby negatively regulating signalling pathways . The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008984:SMAD/FHA
Smad proteins are signal transducers and transcriptional comodulators of the TGF-beta superfamily of ligands.hich play a central role in regulating a broad range of cellular responses.ncluding cell growth.ifferentiation.nd specification of developmental fate.n diverse organisms from C. elegans to humans. Ligand binding to specific transmembrane receptor kinases induces receptor oligomerization and phosphorylation of the receptor specific Smad protein (R-Smad) in the cytoplasm. The R-Smad proteins regulate distinct signaling pathways. Smad1. and 8 mediate the signals of bone morphogenetic proteins (BMPs).hile Smad2 and 3 mediate the signals of activins and TGF-betas. Upon ligand stimulation.-Smad proteins are phosphorylated at the conserved C-terminal tail sequence.S*xS* (where S* denotes a site of phosphorylation). The phosphorylated states of R-Smad proteins form heteromeric complexes with Smad4 and are translocated into the nucleus. In the nucleus.he heteromeric complexes function as gene-specific transcription activators by binding to promoters and interacting with transcriptional coactivators. Smad6 and Smad7 are inhibitory Smad proteins that inhibit TGF-beta signaling by interfering with either receptor-mediated phosphorylation or hetero-oligomerization between Smad4 and R-Smad proteins. Smad proteins comprise two conserved MAD homology domains.ne in the N-terminus (MH1) and one in the C-terminus (MH2).eparated by a more variable.roline-rich linker region. The MH1 domain has a role in DNA binding and negatively regulates the functions of MH2 domain.hereas the MH2 domain is responsible for transactivation and mediates phosphorylation-triggered heteromeric assembly between Smad4 and R-Smad . The MH1 domain adopts a compact globular fold.ith four alpha helices.ix short beta strands.nd five loops. The N-terminal half of the sequence consists of three alpha helices.nd the C-terminal half contains all six beta strands.hich form two small beta sheets and one beta hairpin. The fourth alpha helix is located in the hydrophobic core of the molecule.urrounded by the N-terminal three alpha helices on one side and by the two small beta sheets and the beta hairpin on the other side. These secondary structural elements are connected with five intervening surface loops. The MH1 domain employs a novel DNA-binding motif.n 11-residue beta-hairpin formed by strands B2 and B3.o contact DNA in the major groove. Two residues in the L3 loop and immediately preceding strand B2 also contribute significantly to DNA recognition. The beta hairpin appears to protrude outward from the globular MH1 core .
  IPR013019:MAD homology, MH1
This family of proteins was first identified in Caenorhabditis elegans. Mammalian dwarfins arephosphorylated in response to transforming growth factor beta and are implicated in control of cell growth . The dwarfin family also includes the Drosophila protein MAD that is required for the function of decapentaplegic (DPP) and may play a role in DPP signaling. Drosophila Mad binds to DNA and directly mediates activation of vestigial by Dpp .
  IPR013790:Dwarfin
IPR001132:MH2 
Evalue:-120.443695068359 
Location:265-443IPR003619:DWA 
Evalue:-67.1487416512809 
Location:25-134
SequencesProtein: SMAD1_HUMAN (465 aa)
mRNA: NM_005900
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentK04676
  Level 3 annotation:
    SMAD, mothers against DPP 1/5/8
  Level 2 annotation:
    TGF-beta signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 81 residues, 146622400-146622640Exon2: 194 residues, 146655039-146655615Exon3: 88 residues, 146680405-146680663Exon4: 41 residues, 146683183-146683300Exon5: 76 residues, 146687304-146687526Exon6: 87 residues, 146694385-146694642Exon7: 462 residues, 146698392-146699773Exon8: 2 residues, -Jump to SMAD1_HUMAN  
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