RecQ-mediated genome instability protein 1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• enzyme activator activity Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Binding and activation of DNA topoisomerase III by the Rmi1 subunit."
    Chen C.F., Brill S.J.
    J. Biol. Chem. 282:28971-28979(2007) [PubMed] [Europe PMC] [Abstract]
• four-way junction DNA binding Source: SGDInferred from direct assayⁱ
  • Ref.7

    "Yeast Rmi1/Nce4 controls genome stability as a subunit of the Sgs1-Top3 complex."
    Mullen J.R., Nallaseth F.S., Lan Y.Q., Slagle C.E., Brill S.J.
    Mol. Cell. Biol. 25:4476-4487(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH SGS1 AND TOP3.
• single-stranded DNA binding Source: SGDInferred from direct assayⁱ
  • Ref.7

    "Yeast Rmi1/Nce4 controls genome stability as a subunit of the Sgs1-Top3 complex."
    Mullen J.R., Nallaseth F.S., Lan Y.Q., Slagle C.E., Brill S.J.
    Mol. Cell. Biol. 25:4476-4487(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH SGS1 AND TOP3.

GO - Biological processⁱ

• cell division Source: UniProtKB-KW
• cellular response to DNA damage stimulus Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • Ref.6

    "RMI1/NCE4, a suppressor of genome instability, encodes a member of the RecQ helicase/Topo III complex."
    Chang M., Bellaoui M., Zhang C., Desai R., Morozov P., Delgado-Cruzata L., Rothstein R., Freyer G.A., Boone C., Brown G.W.
    EMBO J. 24:2024-2033(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SGS1 AND TOP3.
• DNA topological change Source: SGDInferred from direct assayⁱ
  • "Decatenation of DNA by the S. cerevisiae Sgs1-Top3-Rmi1 and RPA complex: a mechanism for disentangling chromosomes."
    Cejka P., Plank J.L., Dombrowski C.C., Kowalczykowski S.C.
    Mol. Cell 47:886-896(2012) [PubMed] [Europe PMC] [Abstract]
• meiotic cell cycle Source: UniProtKB-KW
• mitotic sister chromatid cohesion Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Rmi1, a member of the Sgs1-Top3 complex in budding yeast, contributes to sister chromatid cohesion."
    Lai M.S., Seki M., Ui A., Enomoto T.
    EMBO Rep. 8:685-690(2007) [PubMed] [Europe PMC] [Abstract]
  • "Rmi1 functions in S phase-mediated cohesion establishment via a pathway involving the Ctf18-RFC complex and Mrc1."
    Lai M.S., Seki M., Tada S., Enomoto T.
    Biochem. Biophys. Res. Commun. 427:682-686(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of DNA binding Source: SGDInferred from direct assayⁱ
  • "Binding and activation of DNA topoisomerase III by the Rmi1 subunit."
    Chen C.F., Brill S.J.
    J. Biol. Chem. 282:28971-28979(2007) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MSFSSILSQD ITDDITPPAY SATLGSREQI VFRAYQNEPW LAGTASNLIL 
        60         70         80         90        100
DKKLVIVDRE LLFQVLMVEN ITKSKLTQID DIKTKLDPKK QKVDRLRSGA 
       110        120        130        140        150
QGNGAKKYEV ITQVDMEDDG NVADNNCAKE NNSNNNSSAA KNKAVFKLTL 
       160        170        180        190        200
QSKSGDVFFA INSTPISWSS CMLGSKIVIL PGTVFNRGVF ILKDSQVIFL 
       210        220        230        240 
GGINRVWNEN RDQKFCDYLE SKLQRDKQLV NGGSKKRKAN D          

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
2. Yeast chromosome XVI
   Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
3. SIMILARITY comments
   Index of protein domains and families