DNA repair protein rad50

<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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

Sites

Regions

<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

• ATP binding Source: PomBase
• DNA end binding Source: PomBaseInferred from experimentⁱ
  • "Mre11 complex links sister chromatids to promote repair of a collapsed replication fork."
    Zhu M., Zhao H., Limbo O., Russell P.
    Proc Natl Acad Sci U S A 115:8793-8798(2018) [PubMed] [Europe PMC] [Abstract]
• DNA helicase activity Source: PomBase
• double-stranded telomeric DNA binding Source: PomBase
• G-quadruplex DNA binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• single-stranded telomeric DNA binding Source: PomBase

GO - Biological processⁱ

• chromosome organization involved in meiotic cell cycle Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• DNA damage response, detection of DNA damage Source: PomBase <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • Ref.3

    "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint."
    Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.
    Mol. Cell. Biol. 23:6564-6573(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
• DNA duplex unwinding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• DNA strand resection involved in replication fork processing Source: PomBase <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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "The end-joining factor Ku acts in the end-resection of double strand break-free arrested replication forks."
    Teixeira-Silva A., Ait Saada A., Hardy J., Iraqui I., Nocente M.C., Freon K., Lambert S.A.E.
    Nat Commun 8:1982-1982(2017) [PubMed] [Europe PMC] [Abstract]
• double-strand break repair Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• double-strand break repair involved in meiotic recombination Source: PomBaseInferred from mutant phenotypeⁱ
  • "Conserved and nonconserved proteins for meiotic DNA breakage and repair in yeasts."
    Young J.A., Hyppa R.W., Smith G.R.
    Genetics 167:593-605(2004) [PubMed] [Europe PMC] [Abstract]
• double-strand break repair via homologous recombination Source: PomBaseInferred by curatorⁱ
  • Ref.3

    "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint."
    Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.
    Mol. Cell. Biol. 23:6564-6573(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
• double-strand break repair via nonhomologous end joining Source: PomBaseInferred from mutant phenotypeⁱ
  • "The fission yeast MRN complex tethers dysfunctional telomeres for NHEJ repair."
    Reis C.C., Batista S., Ferreira M.G.
    EMBO J 31:4576-4586(2012) [PubMed] [Europe PMC] [Abstract]
• gene conversion at mating-type locus Source: PomBaseInferred from mutant phenotypeⁱ
  • "Mre11 complex links sister chromatids to promote repair of a collapsed replication fork."
    Zhu M., Zhao H., Limbo O., Russell P.
    Proc Natl Acad Sci U S A 115:8793-8798(2018) [PubMed] [Europe PMC] [Abstract]
• intra-S DNA damage checkpoint Source: PomBaseInferred from mutant phenotypeⁱ
  • Ref.3

    "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint."
    Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.
    Mol. Cell. Biol. 23:6564-6573(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
• meiotic DNA double-strand break clipping Source: PomBaseInferred from mutant phenotypeⁱ
  • "Meiotic DNA double-strand break repair requires two nucleases, MRN and Ctp1, to produce a single size class of Rec12 (Spo11)-oligonucleotide complexes."
    Milman N., Higuchi E., Smith G.R.
    Mol Cell Biol 29:5998-6005(2009) [PubMed] [Europe PMC] [Abstract]
  • "Ctp1 and the MRN-complex are required for endonucleolytic Rec12 removal with release of a single class of oligonucleotides in fission yeast."
    Rothenberg M., Kohli J., Ludin K.
    PLoS Genet 5:e1000722-e1000722(2009) [PubMed] [Europe PMC] [Abstract]
• meiotic DNA double-strand break formation Source: PomBaseInferred from mutant phenotypeⁱ
  • "A 160-bp palindrome is a Rad50.Rad32-dependent mitotic recombination hotspot in Schizosaccharomyces pombe."
    Farah J.A., Hartsuiker E., Mizuno K., Ohta K., Smith G.R.
    Genetics 161:461-468(2002) [PubMed] [Europe PMC] [Abstract]
  • "A novel recombination pathway initiated by the Mre11/Rad50/Nbs1 complex eliminates palindromes during meiosis in Schizosaccharomyces pombe."
    Farah J.A., Cromie G., Steiner W.W., Smith G.R.
    Genetics 169:1261-1274(2005) [PubMed] [Europe PMC] [Abstract]
• mitotic recombination-dependent replication fork processing Source: PomBaseInferred from mutant phenotypeⁱ
  • "Recovery of arrested replication forks by homologous recombination is error-prone."
    Iraqui I., Chekkal Y., Jmari N., Pietrobon V., Freon K., Costes A., Lambert S.A.
    PLoS Genet 8:e1002976-e1002976(2012) [PubMed] [Europe PMC] [Abstract]
• mitotic recombination involved in replication fork processing Source: PomBaseInferred from mutant phenotypeⁱ
  • "The end-joining factor Ku acts in the end-resection of double strand break-free arrested replication forks."
    Teixeira-Silva A., Ait Saada A., Hardy J., Iraqui I., Nocente M.C., Freon K., Lambert S.A.E.
    Nat Commun 8:1982-1982(2017) [PubMed] [Europe PMC] [Abstract]
• nucleic acid phosphodiester bond hydrolysis Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of reciprocal meiotic recombination Source: PomBaseInferred from mutant phenotypeⁱ
  • Ref.1

    "Fission yeast Rad50 stimulates sister chromatid recombination and links cohesion with repair."
    Hartsuiker E., Vaessen E., Carr A.M., Kohli J.
    EMBO J. 20:6660-6671(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH RAD21 COHESIN COMPLEX.
• signal transduction involved in DNA damage checkpoint Source: PomBaseInferred by curatorⁱ
  • Ref.3

    "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint."
    Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.
    Mol. Cell. Biol. 23:6564-6573(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
• stalled replication fork localization to nuclear periphery Source: PomBaseInferred from mutant phenotypeⁱ
  • "The nuclear pore primes recombination-dependent DNA synthesis at arrested forks by promoting SUMO removal."
    Kramarz K., Schirmeisen K., Boucherit V., Ait Saada A., Lovo C., Palancade B., Freudenreich C., Lambert S.A.E.
    Nat Commun 11:5643-5643(2020) [PubMed] [Europe PMC] [Abstract]
• telomere maintenance Source: PomBase <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%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Competition between the Rad50 complex and the Ku heterodimer reveals a role for Exo1 in processing double-strand breaks but not telomeres."
    Tomita K., Matsuura A., Caspari T., Carr A.M., Akamatsu Y., Iwasaki H., Mizuno K., Ohta K., Uritani M., Ushimaru T., Yoshinaga K., Ueno M.
    Mol Cell Biol 23:5186-5197(2003) [PubMed] [Europe PMC] [Abstract]
• telomere maintenance via recombination Source: PomBaseInferred from genetic interactionⁱ
  • "Recombination-based telomere maintenance is dependent on Tel1-MRN and Rap1 and inhibited by telomerase, Taz1, and Ku in fission yeast."
    Subramanian L., Moser B.A., Nakamura T.M.
    Mol Cell Biol 28:1443-1455(2008) [PubMed] [Europe PMC] [Abstract]
• telomere maintenance via telomerase Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [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

• UniProt annotation
• GO - Cellular component

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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure 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

Domains and Repeats

Coiled coil

Compositional bias

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<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

Keywords - Domainⁱ

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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
MSCIDRMSIM GIRSFDNRSR ESIQFFSPLT LIVGQNGSGK TTIIECLKYA 
        60         70         80         90        100
TTGILPPNTK GGAFIHDPKI CGEKEVLAQV KLAFRNTNQV KMICTRSLQL 
       110        120        130        140        150
SVKKTTRQQK TLDGQLLILK DNERTTISNR CAELDSQVPL SLGVSKALLD 
       160        170        180        190        200
YVIFCHQEES FWPLSEPANL KKRFDEIFES LRYAKALDQI KGLKRDQETQ 
       210        220        230        240        250
VKVDQATLTH YRSDKERAEK IELRVHESLK RISCIRSKVE ELDQEITETA 
       260        270        280        290        300
RLQDELFKST EEYEQQMITI RHLESQSDII NTTINDLKSQ MTITDESSED 
       310        320        330        340        350
LEKLHSNFAE KVKEEQELYK SLEKKRSDLE SLLKSRRELL EKLTGDLGKI 
       360        370        380        390        400
QGEIESLEKL KVKKSTMINE IVHRYNINEI NEEGIMTEVS KYASLVNKNY 
       410        420        430        440        450
EISSGKLKER QVAVRARIEG IKAHEMFLNN RVSEINSSLE KQLTTQKELR 
       460        470        480        490        500
SRFEILFPVK LQREDFTKDV EKSDLWIKSL RQEYESKNLL ELLDKHQTAL 
       510        520        530        540        550
SSVENRLDEI SEIVDSYHKY SGVRTKLQVF EENKTNKSAI LANQLMTLKS 
       560        570        580        590        600
SFSEVMSYEL KDDDNYNEEL DKLVEDVRKK LQEKEEAESS LRSVRERLEI 
       610        620        630        640        650
RISLSVQSIN DLTENKKIKT KTLKSYSGTF ASMISEIKAL ESEIEENRKT 
       660        670        680        690        700
LHSLQFGSTF YEKAIEICVD QHACQLCQRS LDKEEEKLFV EHCHSMIDVI 
       710        720        730        740        750
PSKSAEVYSH LETLTKTFKN LSEAKPIFDE IELLDKRLSE TKTELSDLQG 
       760        770        780        790        800
DLQGLDIRKD EIQSELDTLY LRRANLEKLQ LLVKDISNLE EEIRTIDRET 
       810        820        830        840        850
EVLRIELPSS IAHHNLDEIY AEREKLLEKR GYLRKQIERT KLEETSFKKK 
       860        870        880        890        900
IDDAVLANNE QKLKLTKLNF QVNELEQLEK DINKSSEDCD LQKKKLLEVS 
       910        920        930        940        950
SKQGSQAPFL NELESEYEKL EADIQEMAQK SRTEILEANE YLHQLNEWNS 
       960        970        980        990       1000
ELRIDVSTKF KCIKEKKSNI GEEVRIIASK IESTDDNLRK LQERLADLRT 
      1010       1020       1030       1040       1050
RERNASDNLR LRALMRQLEE AVTQKNYLLS QQSHDDRESF RERMQILKSK 
      1060       1070       1080       1090       1100
YGALNAERAG LLGECKQLEN SITKDKEELN MEFKDADERF RRQLIKTKTT 
      1110       1120       1130       1140       1150
GKANEDLGKY AKALDVAIMQ LHSMKMNEIN RIVDELWKQT YCGTDIDTIL 
      1160       1170       1180       1190       1200
IRSDSEGKGN RTYNYRVCMV KGDAELDMRG RCSAGQKVLA CIIIRLALAE 
      1210       1220       1230       1240       1250
CLGVNCGILA LDEPTTNLDE ENICSLAKNL SRIVEFRRKQ ANFQLIVITH 
      1260       1270       1280 
DEQFIRLVNS DAYCSYYYRV KRDTNQKSMI VKEPL                 

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

• 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. Schizosaccharomyces pombe
   Schizosaccharomyces pombe: entries and gene names
2. SIMILARITY comments
   Index of protein domains and families