{
  "@type": "dcat:Dataset",
  "accessLevel": "public",
  "bureauCode": [
    "009:25"
  ],
  "contactPoint": {
    "@type": "vcard:Contact",
    "fn": "NIH",
    "hasEmail": "mailto:info@nih.gov"
  },
  "description": "Background:\n          Cohesin is a macromolecular complex that links sister chromatids together at the metaphase plate during mitosis. The links are formed during DNA replication and destroyed during the metaphase-to-anaphase transition. In budding yeast, the 14S cohesin complex comprises at least two classes of SMC (structural maintenance of chromosomes) proteins - Smc1 and Smc3 - and two SCC (sister-chromatid cohesion) proteins - Scc1 and Scc3. The exact function of these proteins is unknown.\n        \n        \n          Results:\n          Searches of protein sequence databases have revealed new homologs of cohesin proteins. In mouse, Mmip1 (Mad member interacting protein 1) and Smc3 share 99% sequence identity and are products of the same gene. A phylogenetic tree of SMC homologs reveals five families: Smc1, Smc2, Smc3, Smc4 and an ancestral family that includes the sequences from the Archaea and Eubacteria. This ancestral family also includes sequences from eukaryotes. A cohesion interaction network, comprising 17 proteins, has been constructed using two proteomic databases. Genes encoding six proteins in the cohesion network share a common upstream region that includes the MluI cell-cycle box (MCB) element. Pairs of the proteins in this network share common sequence motifs that could represent common structural features such as binding sites. Scc2 shares a motif with Chk1 (kinase checkpoint protein), that comprises part of the serine/threonine protein kinase motif, including the active-site residue.\n        \n        \n          Conclusions:\n          We have combined genomic and proteomic data into a comprehensive network of information to reach a better understanding of the function of the cohesin complex. We have identified new SMC homologs, created a new SMC phylogeny and identified shared DNA and protein motifs. The potential for Scc2 to function as a kinase - a hypothesis that needs to be verified experimentally - could provide further evidence for the regulation of sister-chromatid cohesion by phosphorylation mechanisms, which are currently poorly understood.",
  "distribution": [
    {
      "@type": "dcat:Distribution",
      "description": "Visit the original government dataset for complete information, documentation, and data access.",
      "downloadURL": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC30708/",
      "mediaType": "text/html",
      "title": "Official Government Data Source"
    }
  ],
  "identifier": "https://healthdata.gov/api/views/a274-igd2",
  "issued": "2025-07-13",
  "keyword": [
    "cohesin-complex",
    "nih",
    "protein-homology",
    "sister-chromatid-cohesion",
    "smc-proteins"
  ],
  "landingPage": "https://healthdata.gov/d/a274-igd2",
  "modified": "2025-09-06",
  "programCode": [
    "009:033"
  ],
  "publisher": {
    "@type": "org:Organization",
    "name": "National Institutes of Health"
  },
  "theme": [
    "NIH"
  ],
  "title": "The cohesin complex: sequence homologies, interaction networks and shared motifs"
}