# refs

id: PMID:19473263
data:
  {"abstract":"Schizosaccharomyces cells divide by medial septation, followed by enzymatic degradation of parts of the septum (septum cleavage) to allow the sister cells to separate from each other. In a previous study we found that the cell separation mutant sep9-307 was defective in a gene that encodes a protein highly similar in sequence to the Saccharomyces cerevisiae protein Spt8, a subunit of the SAGA complex. Here, we show that the sep9-307 mutation causes a frameshift in translation. The deletion of sep9(+) is not lethal but abolishes normal septum cleavage by reducing the activity of ace2(+), a gene coding for a transcription factor of numerous genes producing proteins for septum cleavage. Indirect evidence indicates that Sep9 might also act directly in the transcription of certain target genes (e.g. eng1(+)) of this regulator. sep9-307 is synthetically lethal with mutations in the cell separation genes sep11/med18(+) and sep15/med8(+), which encode subunits of the general transcription factor mediator. Heterologous expression of SPT8 and the putative Schizosaccharomyces japonicus sep9(+) orthologue cannot substitute for sep9(+). Both Spt8 and the fission yeast proteins have highly acidic (74-76 amino-acid long) N-terminal regions with no sequence conservation.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Batta G, Szilagyi Z, Laczik M, Sipiczki M","authors_abbrev":"Batta G et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"FEMS Yeast Res 2009 Aug;9(5):757-67","cv_annotations":{},"doi":"10.1111/j.1567-1364.2009.00522.x","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2009","pubmed_entrez_date":"2009-05-29","pubmed_publication_date":"Aug 2009","terms_by_termid":{},"title":"The involvement of the Schizosaccharomyces pombe sep9/spt8 gene in the regulation of septum cleavage.","uniquename":"PMID:19473263"}


id: PMID:32109380
data:
  {"abstract":"Eukaryotic genomes are organized within the nucleus through interactions with inner nuclear membrane (INM) proteins. How chromatin tethering to the INM is controlled in interphase and how this process contributes to subsequent mitotic nuclear envelope (NE) remodeling remains unclear. We have probed these fundamental questions using the fission yeast Schizosaccharomyces japonicus, which breaks and reforms the NE during mitosis. We show that attachments between heterochromatin and the transmembrane Lem2-Nur1 complex at the INM are remodeled in interphase by the ESCRT-III/Vps4 machinery. Failure of ESCRT-III/Vps4 to release Lem2-Nur1 from heterochromatin leads to persistent association of chromosomes with the INM throughout mitosis. At mitotic exit, such trapping of Lem2-Nur1 on heterochromatin prevents it from re-establishing nucleocytoplasmic compartmentalization. Our work identifies the Lem2-Nur1 complex as a substrate for the nuclear ESCRT machinery and explains how the dynamic tethering of chromosomes to the INM is linked to the establishment of nuclear compartmentalization.","alleles_by_uniquename":{"SJAG_01050:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01050","name":"nur1delta","uniquename":"SJAG_01050:allele-1"},"SJAG_01242:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01242","name":"vps32delta","uniquename":"SJAG_01242:allele-1"},"SJAG_01330:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01330","name":"mad2delta","uniquename":"SJAG_01330:allele-1"},"SJAG_01745:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01745","name":"lem2delta","uniquename":"SJAG_01745:allele-1"},"SJAG_03250:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03250","name":"sst4delta","uniquename":"SJAG_03250:allele-1"},"SJAG_03783:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03783","name":"vps24delta","uniquename":"SJAG_03783:allele-1"},"SJAG_03892:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03892","name":"vps4delta","uniquename":"SJAG_03892:allele-1"},"SJAG_03892:allele-2":{"allele_type":"amino_acid_mutation","description":"E233Q","gene_uniquename":"SJAG_03892","name":"Vps4-EQ","uniquename":"SJAG_03892:allele-2"},"SJAG_03892:allele-3":{"allele_type":"amino_acid_mutation","description":"I307T L327S","gene_uniquename":"SJAG_03892","name":"vps4-ts","uniquename":"SJAG_03892:allele-3"},"SJAG_04349:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04349","name":"vps28delta","uniquename":"SJAG_04349:allele-1"},"SJAG_04489:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04489","name":"did4delta","uniquename":"SJAG_04489:allele-1"},"SJAG_04912:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04912","name":"vps25delta","uniquename":"SJAG_04912:allele-1"},"SJAG_05207:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_05207","name":"cmp7delta","uniquename":"SJAG_05207:allele-1"}},"annotation_curators":[{"annotation_count":53,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-06-17","authors":"Pieper GH, Sprenger S, Teis D, Oliferenko S","authors_abbrev":"Pieper GH et al.","canto_added_date":"2021-05-10 02:37:07","canto_annotation_status":"APPROVED","canto_approved_date":"2021-06-17 17:46:25","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-06-17 17:46:25","canto_session_key":"89c611dbc0229af1","canto_session_submitted_date":"2021-06-17 17:46:16","canto_triage_status":"Curatable","citation":"Dev Cell 2020 04 06;53(1):27-41.e6","cv_annotations":{"cellular_component":[{"annotations":[115165],"is_not":false,"summary":null,"term":"GO:0000781"},{"annotations":[115163],"is_not":false,"summary":null,"term":"GO:0005783"},{"annotations":[115185],"is_not":false,"summary":null,"term":"GO:0000792"},{"annotations":[115190],"is_not":false,"summary":null,"term":"GO:1990343"},{"annotations":[115147],"is_not":false,"summary":null,"term":"GO:0000776"},{"annotations":[115167],"is_not":false,"summary":null,"term":"GO:0005771"},{"annotations":[115169],"is_not":false,"summary":null,"term":"GO:0032585"},{"annotations":[115168,115170],"is_not":false,"summary":null,"term":"GO:0031965"},{"annotations":[115191],"is_not":false,"summary":null,"term":"GO:0005643"},{"annotations":[115148,115153,115171],"is_not":false,"summary":null,"term":"GO:0005816"}],"molecular_function":[{"annotations":[115146],"is_not":false,"summary":null,"term":"GO:0043515"}],"multi_locus_phenotype":[{"annotations":[115176],"is_not":false,"summary":null,"term":"FYPO:0007771"},{"annotations":[115187],"is_not":false,"summary":null,"term":"FYPO:0001132"}],"single_locus_phenotype":[{"annotations":[115172,115173,115174],"is_not":false,"summary":null,"term":"FYPO:0001440"},{"annotations":[115183,115184],"is_not":false,"summary":null,"term":"FYPO:0001370"},{"annotations":[115186],"is_not":false,"summary":null,"term":"FYPO:0004718"},{"annotations":[115151,115152,115158,115159,115161,115162,115175,115177,115178,115179,115180,115181,115182],"is_not":false,"summary":null,"term":"FYPO:0007771"},{"annotations":[115164],"is_not":false,"summary":null,"term":"FYPO:0004318"},{"annotations":[115155],"is_not":false,"summary":null,"term":"FYPO:0007073"},{"annotations":[115149,115150,115156,115157],"is_not":false,"summary":null,"term":"FYPO:0007772"},{"annotations":[115160],"is_not":false,"summary":null,"term":"FYPO:0007770"},{"annotations":[115166],"is_not":false,"summary":null,"term":"FYPO:0003780"},{"annotations":[115154],"is_not":false,"summary":null,"term":"FYPO:0003657"},{"annotations":[115188,115189],"is_not":false,"summary":null,"term":"FYPO:0001234"}]},"doi":"10.1016/j.devcel.2020.01.028","gene_count":15,"genes_by_uniquename":{"SJAG_00684":null,"SJAG_01050":null,"SJAG_01242":null,"SJAG_01330":null,"SJAG_01601":null,"SJAG_01745":null,"SJAG_01777":null,"SJAG_03250":null,"SJAG_03299":null,"SJAG_03783":null,"SJAG_03892":null,"SJAG_04349":null,"SJAG_04489":null,"SJAG_04912":null,"SJAG_05207":null},"genotypes_by_uniquename":{"Vps4-EQ-E233Q-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"Vps4-EQ(E233Q aa)","display_uniquename":"Vps4-EQ-E233Q-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-2","expression":"Not assayed or wild type"}]}]},"cmp7delta":{"display_name":"cmp7delta","display_uniquename":"cmp7delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_05207:allele-1","expression":"Null"}]}]},"cmp7delta__vps4-ts-I307T_L327S-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"cmp7delta vps4-ts(I307T L327S aa)","display_uniquename":"cmp7delta__vps4-ts-I307T_L327S-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_05207:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-3","expression":"Not assayed or wild type"}]}]},"did4delta":{"display_name":"did4delta","display_uniquename":"did4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04489:allele-1","expression":"Null"}]}]},"lem2delta":{"display_name":"lem2delta","display_uniquename":"lem2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01745:allele-1","expression":"Null"}]}]},"mad2delta":{"display_name":"mad2delta","display_uniquename":"mad2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01330:allele-1","expression":"Null"}]}]},"nur1delta":{"display_name":"nur1delta","display_uniquename":"nur1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01050:allele-1","expression":"Null"}]}]},"nur1delta__vps4delta":{"display_name":"nur1delta vps4delta","display_uniquename":"nur1delta__vps4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01050:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-1","expression":"Null"}]}]},"sst4delta":{"display_name":"sst4delta","display_uniquename":"sst4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03250:allele-1","expression":"Null"}]}]},"vps24delta":{"display_name":"vps24delta","display_uniquename":"vps24delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03783:allele-1","expression":"Null"}]}]},"vps25delta":{"display_name":"vps25delta","display_uniquename":"vps25delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04912:allele-1","expression":"Null"}]}]},"vps28delta":{"display_name":"vps28delta","display_uniquename":"vps28delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04349:allele-1","expression":"Null"}]}]},"vps32delta":{"display_name":"vps32delta","display_uniquename":"vps32delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01242:allele-1","expression":"Null"}]}]},"vps4-ts-I307T_L327S-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"vps4-ts(I307T L327S aa)","display_uniquename":"vps4-ts-I307T_L327S-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-3","expression":"Not assayed or wild type"}]}]},"vps4delta":{"display_name":"vps4delta","display_uniquename":"vps4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-1","expression":"Null"}]}]}},"ltp_gene_count":15,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_01242","interactor_uniquename":"SJAG_03892","reference_uniquename":"PMID:32109380","throughput":"low"},{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_04489","interactor_uniquename":"SJAG_03892","reference_uniquename":"PMID:32109380","throughput":"low"},{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_05207","interactor_uniquename":"SJAG_01242","reference_uniquename":"PMID:32109380","throughput":"low"},{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_05207","interactor_uniquename":"SJAG_01745","reference_uniquename":"PMID:32109380","throughput":"low"},{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_05207","interactor_uniquename":"SJAG_03892","reference_uniquename":"PMID:32109380","throughput":"low"}],"publication_year":"2020","pubmed_entrez_date":"2020-02-29","pubmed_publication_date":"06 04 2020","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000137":null,"FYPO:0001132":null,"FYPO:0001234":null,"FYPO:0001370":null,"FYPO:0001440":null,"FYPO:0003657":null,"FYPO:0003780":null,"FYPO:0004318":null,"FYPO:0004718":null,"FYPO:0007073":null,"FYPO:0007770":null,"FYPO:0007771":null,"FYPO:0007772":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"GO:0000093":null,"GO:0000776":null,"GO:0000781":null,"GO:0000792":null,"GO:0000815":null,"GO:0005643":null,"GO:0005771":null,"GO:0005783":null,"GO:0005816":null,"GO:0031965":null,"GO:0032585":null,"GO:0043515":null,"GO:1990343":null},"title":"ESCRT-III/Vps4 Controls Heterochromatin-Nuclear Envelope Attachments.","uniquename":"PMID:32109380"}


id: GO_REF:0000066
data:
  {"abstract":"We have created a standard template for classes describing the transport of a chemical entity (ChEBI) as a molecular function. The underlying equivalence axiom template is \"GO:0005215 and 'transports or maintains localization of' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of transport of a chemical entity as molecular function in the Gene Ontology","uniquename":"GO_REF:0000066"}


id: PMID:37457408
data:
  {"abstract":"The online version contains supplementary material available at 10.1007/s10068-023-01265-6.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Choi J, Park SY, Park MK, Kim YS, Ahn C, Kim YJ, Park CS","authors_abbrev":"Choi J et al.","canto_added_date":"2023-07-18 00:40:02","canto_curator_role":"JaponicusDB","canto_triage_status":"Biotech","citation":"Food Sci Biotechnol 2023 Sep;32(10):1383-1393","cv_annotations":{},"doi":"10.1007/s10068-023-01265-6","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-07-17","pubmed_publication_date":"Sep 2023","terms_by_termid":{},"title":"Application of  Schizosaccharomyces japonicus  in  makgeolli  fermentation and its brewing characteristics.","uniquename":"PMID:37457408"}


id: PMID:2226803
data:
  {"abstract":"In the fission yeast Schizosaccharomyces pombe, the enzyme RNAse P copurifies with two RNAs, K1- and K2-RNA, which are identical except for their termini [1] and which are encoded by a single gene [2]. We have undertaken the cloning of the K-RNA genes in related organisms in order to gain comparative structural information. Because the K-RNA sequence is poorly conserved across species, we have cloned the K-RNA genes in the Schizosaccharomyces species S. malidevorans, S. japonicus, S. versatilis, and S. octosporus. Of the 4 species, only S. octosporus contains a K-RNA gene different from that in S. pombe; the gene diverges by 20%. Based on the two sequences, nuclease protection data and computer analysis, we have proposed a secondary structure model for the K-RNA. Northern analysis shows the K-RNA genes in all four Schizosaccharomyces species to be expressed as two RNAs, as in S. pombe.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Zimmerly S, Gamulin V, Burkard U, Söll D","authors_abbrev":"Zimmerly S et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"FEBS Lett 1990 Oct 01;271(1-2):189-93","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1990","pubmed_entrez_date":"1990-10-01","pubmed_publication_date":"01 Oct 1990","terms_by_termid":{},"title":"The RNA component of RNase P in Schizosaccharomyces species.","uniquename":"PMID:2226803"}


id: PMID:37164017
data:
  {"abstract":"Most eukaryotes respire oxygen, using it to generate biomass and energy. However, a few organisms have lost the capacity to respire. Understanding how they manage biomass and energy production may illuminate the critical points at which respiration feeds into central carbon metabolism and explain possible routes to its optimization. Here, we use two related fission yeasts, Schizosaccharomyces pombe and Schizosaccharomyces japonicus, as a comparative model system. We show that although S. japonicus does not respire oxygen, unlike S. pombe, it is capable of efficient NADH oxidation, amino acid synthesis, and ATP generation. We probe possible optimization strategies through the use of stable isotope tracing metabolomics, mass isotopologue distribution analysis, genetics, and physiological experiments. S. japonicus appears to have optimized cytosolic NADH oxidation via glycerol-3-phosphate synthesis. It runs a fully bifurcated TCA pathway, sustaining amino acid production. Finally, we propose that it has optimized glycolysis to maintain high ATP/ADP ratio, in part by using the pentose phosphate pathway as a glycolytic shunt, reducing allosteric inhibition of glycolysis and supporting biomass generation. By comparing two related organisms with vastly different metabolic strategies, our work highlights the versatility and plasticity of central carbon metabolism in eukaryotes, illuminating critical adaptations supporting the preferential use of glycolysis over oxidative phosphorylation.","alleles_by_uniquename":{"SJAG_00409:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00409","name":"gpd1delta","uniquename":"SJAG_00409:allele-1"},"SJAG_00601:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00601","name":"rip1delta","uniquename":"SJAG_00601:allele-1"},"SJAG_01355:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01355","name":"cox6delta","uniquename":"SJAG_01355:allele-1"},"SJAG_01753:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01753","name":"mdh1delta","uniquename":"SJAG_01753:allele-1"},"SJAG_02796:allele-1":{"allele_type":"amino_acid_mutation","description":"A343T","gene_uniquename":"SJAG_02796","name":"pyk1-A343T","uniquename":"SJAG_02796:allele-1"},"SJAG_03920:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03920","name":"sdh3delta","uniquename":"SJAG_03920:allele-1"},"SJAG_04843:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04843","name":"fum1delta","uniquename":"SJAG_04843:allele-1"}},"annotation_curators":[{"annotation_count":20,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2023-05-18","authors":"Alam S, Gu Y, Reichert P, Bähler J, Oliferenko S","authors_abbrev":"Alam S et al.","canto_added_date":"2023-05-12 00:40:04","canto_annotation_status":"APPROVED","canto_approved_date":"2023-05-18 12:11:55","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2023-05-18 12:11:54","canto_session_key":"94bcbfb72cf94809","canto_session_submitted_date":"2023-05-18 12:11:43","canto_triage_status":"Curatable","citation":"Curr Biol 2023 Apr 30;","cv_annotations":{"single_locus_phenotype":[{"annotations":[115247],"is_not":false,"summary":null,"term":"FYPO:0007363"},{"annotations":[115245],"is_not":false,"summary":null,"term":"FYPO:0000026"},{"annotations":[115244],"is_not":false,"summary":null,"term":"FYPO:0001355"},{"annotations":[115246],"is_not":false,"summary":null,"term":"FYPO:0001489"},{"annotations":[115248],"is_not":false,"summary":null,"term":"FYPO:0004165"},{"annotations":[115242,115243],"is_not":false,"summary":null,"term":"FYPO:0007790"},{"annotations":[115236,115239],"is_not":false,"summary":null,"term":"FYPO:0000760"},{"annotations":[115238,115241],"is_not":false,"summary":null,"term":"FYPO:0000579"},{"annotations":[115237,115240],"is_not":false,"summary":null,"term":"FYPO:0000590"},{"annotations":[115233,115234,115235],"is_not":false,"summary":null,"term":"FYPO:0001357"},{"annotations":[115232],"is_not":false,"summary":null,"term":"FYPO:0001234"},{"annotations":[115249,115250,115251],"is_not":false,"summary":null,"term":"FYPO:0002058"}]},"doi":"10.1016/j.cub.2023.04.046","gene_count":7,"genes_by_uniquename":{"SJAG_00409":null,"SJAG_00601":null,"SJAG_01355":null,"SJAG_01753":null,"SJAG_02796":null,"SJAG_03920":null,"SJAG_04843":null},"genotypes_by_uniquename":{"cox6delta":{"display_name":"cox6delta","display_uniquename":"cox6delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01355:allele-1","expression":"Null"}]}]},"fum1delta":{"display_name":"fum1delta","display_uniquename":"fum1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04843:allele-1","expression":"Null"}]}]},"gpd1delta":{"display_name":"gpd1delta","display_uniquename":"gpd1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00409:allele-1","expression":"Null"}]}]},"mdh1delta":{"display_name":"mdh1delta","display_uniquename":"mdh1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01753:allele-1","expression":"Null"}]}]},"pyk1-A343T-A343T-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"pyk1-A343T(aa)","display_uniquename":"pyk1-A343T-A343T-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02796:allele-1","expression":"Not assayed or wild type"}]}]},"rip1delta":{"display_name":"rip1delta","display_uniquename":"rip1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00601:allele-1","expression":"Null"}]}]},"sdh3delta":{"display_name":"sdh3delta","display_uniquename":"sdh3delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03920:allele-1","expression":"Null"}]}]}},"ltp_gene_count":7,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-05-10","pubmed_publication_date":"30 Apr 2023","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000015":null,"FYECO:0000126":null,"FYECO:0000137":null,"FYPO:0000026":null,"FYPO:0000579":null,"FYPO:0000590":null,"FYPO:0000760":null,"FYPO:0001234":null,"FYPO:0001355":null,"FYPO:0001357":null,"FYPO:0001489":null,"FYPO:0002058":null,"FYPO:0004165":null,"FYPO:0007363":null,"FYPO:0007790":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null},"title":"Optimization of energy production and central carbon metabolism in a non-respiring eukaryote.","uniquename":"PMID:37164017"}


id: PMID:5315726
data:
  {"abstract":"","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bulder CJ","authors_abbrev":"Bulder CJ","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Antonie Van Leeuwenhoek 1971;37(3):353-8","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1971","pubmed_entrez_date":"1971-01-01","pubmed_publication_date":"1971","terms_by_termid":{},"title":"Anaerobic growth, ergosterol content and sensitivity to a polyene antibiotic, of the yeast Schizosaccharomyces japonicus.","uniquename":"PMID:5315726"}


id: GO_REF:0000034
data:
  {"abstract":"Skeletal cell terms and relationships were added and revised at the Skeletal Anatomy Jamboree held by Phenoscape (NSF grant BDI-0641025) and hosted by the National Evolutionary Synthesis Center (NESCent), April 9-10, 2010.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Brian K. Hall (Dalhousie University), Matthew Vickaryous (Ontario Veterinary College, University of Guelph), David Blackburn, University of Kansas; Wasila Dahdul, University of South Dakota and NESCent; Alexander Diehl, Mouse Genome Informatics (MGI); Melissa Haendel, Oregon Health Sciences University; John G. Lundberg, Department of Ichthyology, Academy of Natural Sciences, Philadelphia; Paula Mabee, Department of Biology, University of South Dakota; Martin Ringwald, Mouse Genome Informatics (MGI); Erik Segerdell, Oregon Health Sciences University; Ceri Van Slyke, Zebrafish Information Network (ZFIN); Monte Westerfield, Zebrafish Information Network (ZFIN) and Institute of Neuroscience, University of Oregon.","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Phenoscape Skeletal Anatomy Jamboree","uniquename":"GO_REF:0000034"}


id: GO_REF:0000078
data:
  {"abstract":"We have created a standard template for classes describing the transport or vesicle-mediated transport of a chemical entity (ChEBI) from and/or to a cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0006810 and 'transports or maintains localization of' some X [ and 'has_target_start_location' some F] [ and 'has_target_end_location' some T]\" (transport) and \"GO:0016192 and 'transports or maintains localization of' some X [ and 'has_target_start_location' some F] [ and 'has_target_end_location' some T]\" (vesicle-mediated transport), where F and T are cellular components and X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation for the transport or vesicle-mediated transport of a chemical from and/or to a cell component as biological process in the Gene Ontology","uniquename":"GO_REF:0000078"}


id: PMID:12402243
data:
  {"abstract":"The structure and localization of the microtubule organization centres (MTOCs) of the fission yeast Schizosaccharomyces japonicus var. japonicus were examined by fluorescence microscopy and electron microscopy. Spindle pole bodies (SPBs), which are the fungal equivalent of centrosomes, of Sz. japonicus were visualized by immunofluorescent staining using a monoclonal anti-gamma-tubulin antibody. The behaviour of the SPBs during the cell cycle mostly coincided with previous reports on the most widely used fission yeast Schizosaccharomyces pombe. We cloned the gamma-tubulin gene from Sz. japonicus by PCR using redundant sets of primers corresponding to conserved regions of known gamma-tubulins. The predicted amino acid sequence of Sz. japonicus gamma-tubulin was most similar to the Sz. pombe gamma-tubulin. Under the electron microscope, the SPBs of Sz. japonicus were detected as electron-dense multilayered structures located just outside the nuclear envelope. The SPBs of Sz. japonicus were composed of three electron-dense layers and were surrounded by fuzzy material. Each layer showed structural changes according to the progression of the cell cycle. In mitotic cells, the SPBs were located on the fenestrae of the nuclear envelopes through which the mitotic spindle microtubules ran into the nucleoplasm. Our results show that Sz. japonicus is a very potent and attractive organism for the investigation of the microtubule nucleation system and morphogenesis in yeasts. The Accession No. for the nucleotide sequence of the Sz. japonicus gtb1(+) gene is AF159163.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Horio T, Kimura N, Basaki A, Tanaka Y, Noguchi T, Akashi T, Tanaka K","authors_abbrev":"Horio T et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Yeast 2002 Nov;19(15):1335-50","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2002","pubmed_entrez_date":"2002-10-29","pubmed_publication_date":"Nov 2002","terms_by_termid":{},"title":"Molecular and structural characterization of the spindle pole bodies in the fission yeast Schizosaccharomyces japonicus var japonicus.","uniquename":"PMID:12402243"}


id: GO_REF:0000089
data:
  {"abstract":"We have created a standard template for classes describing the single-organism and multi-organism biological processes. The underlying equivalence axiom templates are \"P and 'bearer_of' some PATO:0002487\" (single-organism) and \"P and 'bearer_of' some PATO:0002486\" (multi-organism), where P is a biological process.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of single-organism and multi-organism biological processes in the Gene Ontology","uniquename":"GO_REF:0000089"}


id: PMID:32140970
data:
  {"abstract":"In eukaryotes, chromosome ends (telomeres) are tethered to the inner nuclear membrane. During the early stages of meiosis, telomeres move along the nuclear membrane and gather near the spindle-pole body, resulting in a bouquet-like arrangement of chromosomes. This chromosomal configuration appears to be widely conserved among eukaryotes, and is assumed to play an important role in the normal progression of meiosis, by mediating the proper pairing of homologous chromosomes. In fission yeast, the Bqt1-Bqt2 protein complex plays a key role in tethering the telomere to the inner nuclear membrane. However, the structural details of the complex required to clarify how telomeres are gathered near the spindle-pole body remain enigmatic. Previously, we devised a preparation procedure for the Schizosaccharomyces japonicus Bqt1-Bqt2 complex, in which a SUMO tag was fused to the N-terminus of the Bqt1 protein. This allowed us to purify the Bqt1-Bqt2 complex from the soluble fraction. In the present study, we found that a maltose-binding protein homolog, Athe_0614, served as a better fusion partner than the SUMO protein, resulting in the marked increase in the solubility of the Bqt1-Bqt2 complex. The Athe_0614 fusion partner may open up new avenues for X-ray crystallographic analyses of the structure of the Bqt1-Bqt2 complex.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Yuzurihara H, Aizawa Y, Saotome M, Ichikawa Y, Yokoyama H, Chikashige Y, Haraguchi T, Hiraoka Y, Kurumizaka H, Kagawa W","authors_abbrev":"Yuzurihara H et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Protein J 2020 04;39(2):174-181","cv_annotations":{},"doi":"10.1007/s10930-020-09887-z","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2020","pubmed_entrez_date":"2020-03-07","pubmed_publication_date":"04 2020","terms_by_termid":{},"title":"Improved Methods for Preparing the Telomere Tethering Complex Bqt1-Bqt2 for Structural Studies.","uniquename":"PMID:32140970"}


id: PMID:31150379
data:
  {"abstract":"Quorum sensing (QS), a mechanism of microbial communication dependent on cell density, governs developmental decisions in many bacteria and in some pathogenic and non-pathogenic fungi including yeasts. In these simple eukaryotes this response is mediated by the release into the growth medium of quorum-sensing molecules (QSMs) whose concentration increases proportionally to the population density. To date the occurrence of QS is restricted to a few yeast species. We show that a QS mediated by the aromatic alcohols phenylethanol and tryptophol represses the dimorphic yeast to hypha differentiation in the fission yeast S. japonicus in response to an increased population density. In addition, the stress activated MAPK pathway (SAPK), which controls cell cycle progression and adaptation to environmental changes in this organism, constitutively represses yeast to hypha differentiation both at transcriptional and post-translational levels. Moreover, deletion of its main effectors Sty1 MAPK and Atf1 transcription factor partially suppressed the QS-dependent block of hyphal development under inducing conditions. RNAseq analysis showed that the expression of nrg1+, which encodes a putative ortholog of the transcription factor Nrg1 that represses yeast to hypha dimorphism in C. albicans, is downregulated both by QS and the SAPK pathway. Remarkably, Nrg1 may act in S. japonicus as an activator of hyphal differentiation instead of being a repressor. S. japonicus emerges as an attractive and amenable model organism to explore the QS mechanisms that regulate cellular differentiation in fungi.","alleles_by_uniquename":{"SJAG_00124:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00124","name":"SJAG_00124delta","uniquename":"SJAG_00124:allele-1"},"SJAG_00266:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00266","name":"atf1delta","uniquename":"SJAG_00266:allele-1"},"SJAG_02013:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02013","name":"pyp1delta","uniquename":"SJAG_02013:allele-1"},"SJAG_02592:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02592","name":"sty1delta","uniquename":"SJAG_02592:allele-1"}},"annotation_curators":[{"annotation_count":37,"community_curator":true,"file_name":null,"file_type":null,"name":"Elisa Gómez Gil","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-08-04","authors":"Gómez-Gil E, Franco A, Madrid M, Vázquez-Marín B, Gacto M, Fernández-Breis J, Vicente-Soler J, Soto T, Cansado J","authors_abbrev":"Gómez-Gil E et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-08-04 11:11:18","canto_curator_name":"Elisa Gómez Gil","canto_curator_role":"community","canto_first_approved_date":"2021-08-04 11:11:18","canto_session_key":"0da7a90b15f75d86","canto_session_submitted_date":"2021-08-03 17:26:10","canto_triage_status":"Curatable","citation":"PLoS Genet 2019 05;15(5):e1008192","cv_annotations":{"PSI-MOD":[{"annotations":[115258,115259,115260,115261],"is_not":false,"summary":null,"term":"MOD:00046"}],"multi_locus_phenotype":[{"annotations":[115286],"is_not":false,"summary":null,"term":"FYPO:0007779"}],"single_locus_phenotype":[{"annotations":[115254,115266],"is_not":false,"summary":null,"term":"FYPO:0004481"},{"annotations":[115282],"is_not":false,"summary":null,"term":"FYPO:0007778"},{"annotations":[115281,115284],"is_not":false,"summary":null,"term":"FYPO:0007776"},{"annotations":[115265],"is_not":false,"summary":null,"term":"FYPO:0000708"},{"annotations":[115283,115285],"is_not":false,"summary":null,"term":"FYPO:0007780"},{"annotations":[115287,115288],"is_not":false,"summary":null,"term":"FYPO:0007824"},{"annotations":[115252,115264],"is_not":false,"summary":null,"term":"FYPO:0001122"},{"annotations":[115276,115280],"is_not":false,"summary":null,"term":"FYPO:0007777"},{"annotations":[115275,115279],"is_not":false,"summary":null,"term":"FYPO:0007775"},{"annotations":[115274,115278],"is_not":false,"summary":null,"term":"FYPO:0007774"},{"annotations":[115277],"is_not":false,"summary":null,"term":"FYPO:0007779"},{"annotations":[115257,115269],"is_not":false,"summary":null,"term":"FYPO:0000097"},{"annotations":[115256,115268],"is_not":false,"summary":null,"term":"FYPO:0000726"},{"annotations":[115255,115267],"is_not":false,"summary":null,"term":"FYPO:0000271"},{"annotations":[115270],"is_not":false,"summary":null,"term":"FYPO:0000841"},{"annotations":[115253],"is_not":false,"summary":null,"term":"FYPO:0000280"},{"annotations":[115273],"is_not":false,"summary":null,"term":"FYPO:0000648"}]},"doi":"10.1371/journal.pgen.1008192","gene_count":4,"genes_by_uniquename":{"SJAG_00124":null,"SJAG_00266":null,"SJAG_02013":null,"SJAG_02592":null},"genotypes_by_uniquename":{"SJAG_00124delta":{"display_name":"SJAG_00124delta","display_uniquename":"SJAG_00124delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00124:allele-1","expression":"Null"}]}]},"SJAG_00124delta__sty1delta":{"display_name":"SJAG_00124delta sty1delta","display_uniquename":"SJAG_00124delta__sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00124:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]},"atf1delta":{"display_name":"atf1delta","display_uniquename":"atf1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00266:allele-1","expression":"Null"}]}]},"pyp1delta":{"display_name":"pyp1delta","display_uniquename":"pyp1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02013:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]}},"ltp_gene_count":4,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2019","pubmed_entrez_date":"2019-06-01","pubmed_publication_date":"05 2019","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000078":null,"FYECO:0000137":null,"FYECO:0000207":null,"FYECO:0000272":null,"FYECO:0000314":null,"FYPO:0000097":null,"FYPO:0000271":null,"FYPO:0000280":null,"FYPO:0000648":null,"FYPO:0000708":null,"FYPO:0000726":null,"FYPO:0000841":null,"FYPO:0001122":null,"FYPO:0004481":null,"FYPO:0007774":null,"FYPO:0007775":null,"FYPO:0007776":null,"FYPO:0007777":null,"FYPO:0007778":null,"FYPO:0007779":null,"FYPO:0007780":null,"FYPO:0007824":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null,"GO:0034599":null,"GO:0034605":null,"GO:0071475":null,"GO:1904547":null,"MOD:00046":null},"title":"Quorum sensing and stress-activated MAPK signaling repress yeast to hypha transition in the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:31150379"}


id: GO_REF:0000047
data:
  {"abstract":"This describes a method for supplying a NOT-qualified, IKR-evidenced GO annotation to a gene product, when general sequence homology considerations would suggest a function or location, or a role in a biological process, but where a curator has determined that the absence of key sequence residues, known to be required for an expected activity or location, indicating the gene product is unlikely to be able to carry out the implied activity, involvement in a process or cellular component location. This reference should only be used used when an IKR-evidenced annotation is made based on curator judgement from manually reviewing the sequence of the gene product and where no publication can be found to support the curators conclusion. It is preferable to cite a peer-reviewed publication (such as a PubMed identifier) for IKR-evidenced annotations whenever possible. Curators will have carefully reviewed the sequence of the annotated protein, and established that the key residues known to be required for an expected activity or location are not present. Inclusion of an identifier in the 'with/from' field, that highlights to the user the lacking residues(e.g. an alignment, domain or rule identifier) is absolutely required when annotating to IKR with this GO_REF. Documentation on the GOC website provides more details on the <a href = \"http://www.geneontology.org/GO.evidence.shtml#ikr\">correct use of the IKR evidence code</a>.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Gene Ontology annotation based on absence of key sequence residues.","uniquename":"GO_REF:0000047"}


id: GO_REF:0000108
data:
  {"abstract":"GO terms are automatically assigned based on inter-ontology links to generate inferred annotations. Annotations from Molecular Function to Biological Process can be propagated, as well as between Biological Process and Cellular Component. Annotations that are created using this inference method receive either the evidence code ECO:0000366 (evidence based on logical inference from automatic annotation used in automatic assertion) or ECO:0000364 (evidence based on logical inference from manual annotation used in automatic assertion), depending on whether the source annotation has a manual or automatic evidence code. Both of these codes map up to the GO Inferred from Electronic Annotation (IEA) evidence code.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GOA 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id: PMID:22572960
data:
  {"abstract":"The aim of mitosis is to produce two daughter nuclei, each containing a chromosome complement identical to that of the mother nucleus. This can be accomplished through a variety of strategies, with \"open\" and \"closed\" modes of mitosis positioned at the opposite ends of the spectrum and a range of intermediate patterns in between. In the \"closed\" mitosis, the nuclear envelope remains intact throughout the nuclear division. In the \"open\" division type, the envelope of the original nucleus breaks down early in mitosis and reassembles around the segregated daughter genomes. In any case, the nuclear membrane has to remodel to accommodate the mitotic spindle assembly, chromosome segregation and formation of the daughter nuclei. We have recently shown that within the fission yeast clade, the mitotic control of the nuclear surface area may determine the choice between the nuclear envelope breakdown and a fully \"closed\" division. Here we discuss our data and argue that comparative cell biology studies using two fission yeast species, Schizosaccharomyces pombe and Schizosaccharomyces japonicus, could provide unprecedented insights into physiology and evolution of mitosis.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Gu Y, Yam C, Oliferenko S","authors_abbrev":"Gu Y et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Nucleus 2012 May;3(3):220-5","cv_annotations":{},"doi":"10.4161/nucl.19514","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2012","pubmed_entrez_date":"2012-05-11","pubmed_publication_date":"May 2012","terms_by_termid":{},"title":"Divergence of mitotic strategies in fission yeasts.","uniquename":"PMID:22572960"}


id: GO_REF:0000114
data:
  {"abstract":"Method for transferring manual annotations to an entry based on a curator's judgment of its similarity to a putative homolog that has annotations that are supported with experimental evidence. Annotations are created when a curator judges that the sequence, composition and function of a complex shows high similarity to another complex that has annotation(s) supported by experimental evidence (and therefore display one of the evidence codes ECO:0000353 [IPI] or ECO:0005543). Annotations resulting from the transfer of GO terms display the ECO:0005610, ECO:0005544 or ECO:0005546 evidence codes and include an accession for the complex from which the annotation was projected in the 'with/from' field (column 8). This field MUST contain a Complex Portal accession identifier. Putative homologs are chosen using information combined from a variety of complementary sources. Potential homologs are initially identified using sequence similarity search programs such as BLAST. Homologous relationships are then verified manually using a combination of resources including sequence analysis tools, phylogenetic and comparative genomics databases such as Ensembl Compara, INPARANOID and OrthoMCL, as well as other specialised databases such as species-specific collections (e.g. HGNC's HCOP). In all cases curators check the alignments for each complex component and use their experience to assess whether similarity is considered to be strong enough to infer that the two proteins have a common function so that they can confidently project an annotation. While there is no fixed cut-off point in percentage sequence similarity, generally proteins which have greater than 70% identity that covers greater than 90% of the length of both proteins are examined further. Whilst we expect subunit composition to be conserved between closely related species, this is not an absolute rule and orthologous complexes may differ if a subunit cannot be traced in one species or is experimentally shown not to be present. When there is evidence of multiple paralogs for a single species, multiple variants of the complex can be inferred.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Birgit Meldal and Sandra Orchard (1). (1) European Bioinformatics Institute (EBI), Hinxton, Cambridgeshire, United Kingdom","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Manual transfer of experimentally-verified manual GO annotation data to homologous complexes by curator judgment of sequence, composition and function similarity","uniquename":"GO_REF:0000114"}


id: PMID:20737410
data:
  {"abstract":"Schizosaccharomyces japonicus is a fission yeast for which new genetic tools have recently been developed. Here, we report novel plasmid vectors with high transformation efficiency and an electroporation method for Sz. japonicus. We isolated 44 replicating segments from 12 166 transformants of Sz. japonicus genomic fragments and found a chromosomal fragment, RS1, as a new replicating sequence that conferred high transformation activity to Sz. japonicus cells. This sequence was cloned into a pUC19 vector with ura4(+) of Sz. pombe (pSJU11) or the kan gene on the kanMX6 module (pSJK11) as selection markers. These plasmids transformed Sz. japonicus cells in the early-log phase by electroporation at a frequency of 123 cfu/µg for pSJK11 and 301 cfu/µg for pSJU11, which were higher than previously reported autonomously replicating sequences. Although a portion of plasmids remained in host cells by integration into the chromosome via RS1 segment, the plasmids could be recovered from transformants. The plasmid copy number was estimated to be 1.88 copies per cell by Southern blot analysis using a Sz. pombe ura4(+) probe. The plasmid containing ade6(+) suppressed the auxotrophic growth of the ade6-domE mutant, indicating that the plasmid would be useful for suppressor screening and complementation assays in Sz. japonicus. Furthermore, pSJU11 transformed Sz. pombe cells with the same frequency as the pREP2 plasmid. This study is a report to demonstrate practical use of episomal plasmid vectors for genetic research in Sz. japonicus.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Aoki K, Nakajima R, Furuya K, Niki H","authors_abbrev":"Aoki K et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Yeast 2010 Dec;27(12):1049-60","cv_annotations":{},"doi":"10.1002/yea.1815","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2010","pubmed_entrez_date":"2010-08-26","pubmed_publication_date":"Dec 2010","terms_by_termid":{},"title":"Novel episomal vectors and a highly efficient transformation procedure for the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:20737410"}


id: PMID:34200466
data:
  {"abstract":"The Rho family of GTPases represents highly conserved molecular switches involved in a plethora of physiological processes. Fission yeast  Schizosaccharomyces pombe  has become a fundamental model organism to study the functions of Rho GTPases over the past few decades. In recent years, another fission yeast species,  Schizosaccharomyces japonicus , has come into focus offering insight into evolutionary changes within the genus. Both fission yeasts contain only six Rho-type GTPases that are spatiotemporally controlled by multiple guanine-nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and whose intricate regulation in response to external cues is starting to be uncovered. In the present review, we will outline and discuss the current knowledge and recent advances on how the fission yeasts Rho family GTPases regulate essential physiological processes such as morphogenesis and polarity, cellular integrity, cytokinesis and cellular differentiation.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Vicente-Soler J, Soto T, Franco A, Cansado J, Madrid M","authors_abbrev":"Vicente-Soler J et al.","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Cells 2021 Jun 07;10(6)","cv_annotations":{},"doi":"10.3390/cells10061422","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-07-02","pubmed_publication_date":"07 Jun 2021","terms_by_termid":{},"title":"The Multiple Functions of Rho GTPases in Fission Yeasts.","uniquename":"PMID:34200466"}


id: GO_REF:0000036
data:
  {"abstract":"The Gene Ontology Consortium uses the IC (Inferred by Curator) evidence code when an annotation cannot be supported by any direct evidence, but can be inferred by GO annotations that have been annotated to the same gene/gene product identifier in conjunction with the curator's knowledge of biology (supporting GO annotations must not be IC-evidenced). In many cases an IC-evidenced annotation simply applies the same reference that was used in the supporting GO annotation.  The use of IC evidence code in an annotation with reference GO_REF:0000036 signifies a curator inferred the GO term based on evidence from multiple sources of evidence/GO annotations. The 'with/from' field in these annotations will therefore supply more than one GO identifier, obtained from the set of supporting GO annotations assigned to the same gene/gene product identifier which cite publicly-available references.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO Annotation working group","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Manual annotations that require more than one source of functional data to support the assignment of the associated GO term","uniquename":"GO_REF:0000036"}


id: GO_REF:0000084
data:
  {"abstract":"We have created a standard template for classes describing the structural organization of a plant structure as a biological process. The underlying equivalence axiom template is \"'anatomical structure arrangement' and 'results in structural organization of' some P\", where P is a plant anatomical entity (PO:0025131).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of plant structural organization as biological process in the Gene Ontology","uniquename":"GO_REF:0000084"}


id: PMID:35049972
data:
  {"abstract":"The survival of eukaryotic organisms during environmental changes is largely dependent on the adaptive responses elicited by signal transduction cascades, including those regulated by the Mitogen-Activated Protein Kinase (MAPK) pathways. The Cell Integrity Pathway (CIP), one of the three MAPK pathways found in the simple eukaryote fission of yeast  Schizosaccharomyces pombe , shows strong homology with mammalian Extracellular signal-Regulated Kinases (ERKs). Remarkably, studies over the last few decades have gradually positioned the CIP as a multi-faceted pathway that impacts multiple functional aspects of the fission yeast life cycle during unperturbed growth and in response to stress. They include the control of mRNA-stability through RNA binding proteins, regulation of calcium homeostasis, and modulation of cell wall integrity and cytokinesis. Moreover, distinct evidence has disclosed the existence of sophisticated interplay between the CIP and other environmentally regulated pathways, including Stress-Activated MAP Kinase signaling (SAPK) and the Target of Rapamycin (TOR). In this review we present a current overview of the organization and underlying regulatory mechanisms of the CIP in  S. pombe , describe its most prominent functions, and discuss possible targets of and roles for this pathway. The evolutionary conservation of CIP signaling in the dimorphic fission yeast  S. japonicus  will also be addressed.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Cansado J, Soto T, Franco A, Vicente-Soler J, Madrid M","authors_abbrev":"Cansado J et al.","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"J Fungi (Basel) 2021 Dec 30;8(1)","cv_annotations":{},"doi":"10.3390/jof8010032","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2022-01-20","pubmed_publication_date":"30 Dec 2021","terms_by_termid":{},"title":"The Fission Yeast Cell Integrity Pathway: A Functional Hub for Cell Survival upon Stress and Beyond.","uniquename":"PMID:35049972"}


id: PMID:7166567
data:
  {"abstract":"The fine structure of ascospore formation in the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus var. japonicus was studied by serial thin-sectioning and electron microscopy. The morphogenetic events were almost the same in both species. Ascospore development was initiated by the formation of the forespore membrane on the cytoplasmic side of the differentiated nucleus-associated organelle (NAO) in the interval between meiosis I and II in S. pombe, or during the post-meiotic nuclear division in S. japonicus, and the process proceeded almost synchronously through the two or four nuclei in the ascus. The forespore membrane developed by fusion of the cytoplasmic vesicles and this was clearly demonstrated in S. japonicus where the behaviour of vesicles involved in the forespore membrane development could be traced as they were marked by the presence of electron-dense granules. The staining technique, by phosphotungustic acid--chromic acid (PTA-CA) after treatment with periodic acid, was used to attempt to elucidate the origin and the nature of the forespore membrane. The method specific to plasmalemma-type membranes stained both ascus and ascospore plasmalemmas; the forespore membrane was not stained at first but developed the same affinity for stain as the plasma membrane in the course of ascospore development. The results suggest that the forespore membrane did not come directly from the ascus plasma membrane, but from another membrane system such as the endoplasmic reticulum. Spore wall material was deposited in the space between the inner and outer leaflets of the forespore membrane.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Tanaka K, Hirata A","authors_abbrev":"Tanaka K et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Cell Sci 1982 Aug;56:263-79","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1982","pubmed_entrez_date":"1982-08-01","pubmed_publication_date":"Aug 1982","terms_by_termid":{},"title":"Ascospore development in the fission yeasts Schizosaccharomyces pombe and S. japonicus.","uniquename":"PMID:7166567"}


id: PMID:28733401
data:
  {"abstract":"Haploid yeast cells mate to form heterozygotes and subsequently undergo meiosis to form spores. This process can be used to produce gene combinations and variants that are useful for genetic analysis. For example, these spores can be used to generate double mutants or to measure genetic distances in a mutational analysis. Here, we describe mating and spore dissection procedures for  Schizosaccharomyces japonicus  cells. Although the overall procedures resemble those used in  Schizosaccharomyces pombe , some differences exist, including the use of EMM2 medium without nitrogen (EMM-N) for mating and the shorter incubation time of 16-20 h for  S. japonicus  cells. Furthermore, the  S. japonicus  zygotes produce eight spores and thus require an \"octad\" analysis.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Furuya K, Niki H","authors_abbrev":"Furuya K et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Cold Spring Harb Protoc 2017 Dec 01;2017(12):pdb.prot091843","cv_annotations":{},"doi":"10.1101/pdb.prot091843","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2017-07-23","pubmed_publication_date":"01 Dec 2017","terms_by_termid":{},"title":"Mating, Spore Dissection, and Selection of Diploid Cells in  Schizosaccharomyces japonicus .","uniquename":"PMID:28733401"}


id: GO_REF:0000119
data:
  {"abstract":"The Alliance of Genome Resources (https://www.alliancegenome.org/) has procedures in place to establish orthology relationships","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"The Gene Ontology Consortium","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs","uniquename":"GO_REF:0000119"}


id: GO_REF:0000109
data:
  {"abstract":"Trypanosomes are exquisitely structured cells in which protein localisation can be extremely informative for likely function. TrypTag is a project using expression of N- and C-terminal mNeonGreen fusion proteins from the endogenous loci to determine the subcellular localisation of every gene in the Trypanosoma brucei genome. GO Cellular Component terms are manually assigned by curators studying fluorescence microscope images of the resulting cells labelled with mNeonGreen fusion proteins. As trypanosomes are a pathogenic basal eukaryote, this will indicate likely function of both highly conserved eukaryote genes and parasite-specific genes. Resource URL: http://www.tryptag.org Protein subcellular localisation images can be viewed on the Tryptag website, e.g. http://www.tryptag.org?id=Tb927.8.1550","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"TrypTag","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Gene Ontology annotation based on curation of genome-wide subcellular localisation of proteins using fluorescent protein tagging in Trypanosoma brucei","uniquename":"GO_REF:0000109"}


id: GO_REF:0000011
data:
  {"abstract":"A Hidden Markov Model (HMM) is a statistical representation of patterns found in a data set. When using HMMs with proteins, the HMM is a statistical model of the patterns of the amino acids found in a multiple alignment of a set of proteins called the \"seed\". Seed proteins are chosen based on sequence similarity to each other. Seed members can be chosen with different levels of relationship to each other. They can be members of a superfamily (ex. ABC transporter, ATP-binding proteins), they can all share the same exact specific function (ex. biotin synthase) or they could share another type of relationship of intermediate specificity (ex. subfamily, domain). New proteins can be scored against the model generated from the seed according to how closely the patterns of amino acids in the new proteins match those in the seed. There are two scores assigned to the HMM which allow annotators to judge how well any new protein scores to the model. Proteins scoring above the \"trusted cutoff\" score can be assumed to be part of the group defined by the seed. Proteins scoring below the \"noise cutoff\" score can be assumed to NOT be a part of the group. Proteins scoring between the trusted and noise cutoffs may be part of the group but may not. One of the important features of HMMs is that they are built from a multiple alignment of protein sequences, not a pairwise alignment. This is significant, since shared similarity between many proteins is much more likely to indicate shared functional relationship than sequence similarity between just two proteins. The usefulness of an HMM is directly related to the amount of care that is taken in chosing the seed members, building a good multiple alignment of the seed members, assessing the level of specificity of the model, and choosing the cutoff scores correctly. In order to properly assess what functional relevance an above-trusted scoring HMM match has to a query, one must carefully determine what the functional scope of the HMM is. If the HMM models proteins that all share the same function then it is likely possible to assign a specific function to high-scoring match proteins based on the HMM. If the HMM models proteins that have a wide variety of functions, then it will not be possible to assign a specific function to the query based on the HMM match, however, depending on the nature of the HMM in question, it may be possible to assign a more general (family or subfamily level) function. In order to determine the functional scope of an HMM, one must carefully read the documentation associated with the HMM. The annotator must also consider whether the function attributed to the proteins in the HMM makes sense for the query based on what is known about the organism in which the query protein resides and in light of any other information that might be available about the query protein. After carefully considering all of these issues the annotator makes an annotation.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Michelle Gwinn, TIGR curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Hidden Markov Models (TIGR)","uniquename":"GO_REF:0000011"}


id: PMID:22641476
data:
  {"abstract":"Measuring relative genetic distances is one of the best ways to locate genetic loci. Here we report the construction of a strains set for genetic mapping in Schizosaccharomyces japonicus, which belongs to the genus Schizosaccharomyces together with the well-studied fission yeast Sz. pombe. We constructed 29 strains that bear a positive-negative selection marker at different loci. The marker was inserted every 500 kb in the genome of Sz. japonicus. Each marker thus becomes a 'scale mark' of a chromosome that behaves like a yardstick. By determining the genetic distances from the inserted markers, the relative location of a genomic mutation can be determined. We also constructed a fosmid library that covers an entire genome of Sz. japonicus. These tools together would facilitate identification and cloning of the gene.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Furuya K, Aoki K, Niki H","authors_abbrev":"Furuya K et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Yeast 2012 Jun;29(6):241-9","cv_annotations":{},"doi":"10.1002/yea.2907","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2012","pubmed_entrez_date":"2012-05-30","pubmed_publication_date":"Jun 2012","terms_by_termid":{},"title":"Construction of an insertion marker collection of Sz. japonicus (IMACS) for genetic mapping and a fosmid library covering its genome.","uniquename":"PMID:22641476"}


id: PMID:28655757
data:
  {"abstract":"Cytokinesis in many eukaryotes involves a tension-generating actomyosin-based contractile ring. Many components of actomyosin rings turn over during contraction, although the significance of this turnover has remained enigmatic. Here, using  Schizosaccharomyces japonicus , we investigate the role of turnover of actin and myosin II in its contraction. Actomyosin ring components self-organize into ∼1-µm-spaced clusters instead of undergoing full-ring contraction in the absence of continuous actin polymerization. This effect is reversed when actin filaments are stabilized. We tested the idea that the function of turnover is to ensure actin filament homeostasis in a synthetic system, in which we abolished turnover by fixing rings in cell ghosts with formaldehyde. We found that these rings contracted fully upon exogenous addition of a vertebrate myosin. We conclude that actin turnover is required to maintain actin filament homeostasis during ring contraction and that the requirement for turnover can be bypassed if homeostasis is achieved artificially.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":5,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-09","authors":"Chew TG, Huang J, Palani S, Sommese R, Kamnev A, Hatano T, Gu Y, Oliferenko S, Sivaramakrishnan S, Balasubramanian MK","authors_abbrev":"Chew TG et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-07-09 13:45:34","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-09 13:45:34","canto_session_key":"5ead7a365a97d8ab","canto_session_submitted_date":"2021-07-09 13:45:28","canto_triage_status":"Curatable","citation":"J Cell Biol 2017 09 04;216(9):2657-2667","cv_annotations":{"cellular_component":[{"annotations":[115289,115290,115291,115292,115293],"is_not":false,"summary":null,"term":"GO:0005826"}]},"doi":"10.1083/jcb.201701104","gene_count":5,"genes_by_uniquename":{"SJAG_01665":null,"SJAG_02431":null,"SJAG_03596":null,"SJAG_03703":null,"SJAG_04498":null},"genotypes_by_uniquename":{},"ltp_gene_count":5,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2017-06-29","pubmed_publication_date":"04 09 2017","terms_by_termid":{"GO:0005826":null},"title":"Actin turnover maintains actin filament homeostasis during cytokinetic ring contraction.","uniquename":"PMID:28655757"}


id: GO_REF:0000079
data:
  {"abstract":"We have created a standard template for classes describing the assembly or disassembly of a cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0022607 and 'results_in_assembly_of' some C\" (assembly) and \"GO:0022411 and 'results_in_disassembly_of' some C\" (disassembly), where C is a cellular component.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of assembly or disassembly of a cell component as biological process in the Gene Ontology","uniquename":"GO_REF:0000079"}


id: PMID:25942548
data:
  {"abstract":"New work shows the anillin-related protein Mid1 does not position the cytokinetic ring in the fission yeast Schizosaccharomyces japonicus, unlike its role in S. pombe. Further analysis suggests the conserved function of Mid1-like anillin proteins may be in scaffolding, not positioning, the cytokinetic ring. ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Moseley JB","authors_abbrev":"Moseley JB","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Curr Biol 2015 May 04;25(9):R364-6","cv_annotations":{},"doi":"10.1016/j.cub.2015.03.017","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-05-06","pubmed_publication_date":"04 May 2015","terms_by_termid":{},"title":"Cytokinesis: does Mid1 have an identity crisis?","uniquename":"PMID:25942548"}


id: GO_REF:0000025
data:
  {"abstract":"Genes in prokaryotic organisms are often arranged in operons. Genes in an operon are all transcribed into one mRNA. Generally the genes in the operons code for proteins that all have related functions. For example, they may be the steps in a biochemical pathway, or they may be the subunits of a protein complex. Often the genes in operons shared between organisms are syntenic; that is, the same genes are in the same order in the operon in different species. When assessing sequence-comparison-based evidence during the process of manual annotation of a genome, it is often the case that some of the genes in the operon will have strong sequence-based evidence while others will have weak evidence. If seen alone, not in the presence of an operon, the weak evidence in question may not be sufficient to make a functional annotation. However, in the presence of an operon in which there is strong evidence for some of the genes, the very presence of the gene in the operon is a strong indication that the gene shares in the process carried out by the operon. If the putative function is one expected to exist for the process in question and particularly if that function has been observed in the same operon in another species, then the annotation should be made. This type of evidence is inferred from the context of the gene in an operon, and therefore the evidence code is IGC \"inferred from genomic context.\"","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Michelle Gwinn, TIGR curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Operon structure as IGC evidence","uniquename":"GO_REF:0000025"}


id: PMID:12527786
data:
  {"abstract":"The fission yeasts are members of the fungal order Schizosaccharomycetales, a candidate deep-diverging group within Ascomycota. Although a great deal of molecular information is available from Schizosaccharomyces pombe, a model eukaryote, very little is available from other members of this group. In order to better characterize mitochondrial genome evolution in this fungal lineage, the mitochondrial DNA (mtDNA) of two additional fission yeasts, Schizosaccharomyces octosporus and Schizosaccharomyces japonicus var. japonicus, was sequenced. Whereas the mtDNA of S.pombe is only 19 431 bp, the mtDNA of S.octosporus is 44 227 bp, and that of S.japonicus var. japonicus is over 80 kb. The size variation of these mtDNAs is due largely to non-coding regions. The gene content in the latter two mtDNAs is almost identical to that of the completely sequenced S.pombe mtDNA, which encodes 25 tRNA species, the large and small mitochondrial ribosomal RNAs (rnl and rns), the RNA component of mitochondrial RNaseP (rnpB), mitochondrial small subunit ribosomal protein 3 (rps3), cytochrome oxidase subunits 1, 2 and 3 (cox1, cox2 and cox3) and ATP-synthase subunits 6, 8 and 9 (atp6, atp8 and atp9). However, trnI2(cau) (C modified to lysidine) is absent in the S.octosporus mtDNA, as are corresponding ATA codons in its protein-coding genes, and rps3 and rnpB are not found in the mtDNA of S.japonicus var. japonicus. The mtDNA of S.octosporus contains five double hairpin elements, the first report of these elements in an ascomycete. This study provides further evidence in favor of the mobility of these elements, and supports their role in mitochondrial genome rearrangement. The results of our phylogenetic analysis support the monophyly of the Schizosaccharomycetales, but question their grouping within the Archiascomycota.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bullerwell CE, Leigh J, Forget L, Lang BF","authors_abbrev":"Bullerwell CE et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Nucleic Acids Res 2003 Jan 15;31(2):759-68","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2003","pubmed_entrez_date":"2003-01-16","pubmed_publication_date":"15 Jan 2003","terms_by_termid":{},"title":"A comparison of three fission yeast mitochondrial genomes.","uniquename":"PMID:12527786"}


id: GO_REF:0000024
data:
  {"abstract":"Method for transferring manual annotations to an entry based on a curator's judgment of its similarity to a putative ortholog that has annotations that are supported with experimental evidence. Annotations are created when a curator judges that the sequence of a protein shows high similarity to another protein that has annotation(s) supported by experimental evidence (and therefore display one of the evidence codes EXP, IDA, IGI, IMP, IPI or IEP). Annotations resulting from the transfer of GO terms display the 'ISS' evidence code and include an accession for the protein from which the annotation was projected in the 'with' field (column 8). This field can contain either a UniProtKB accession or an IPI (International Protein Index) identifier. Only annotations with an experimental evidence code and which do not have the 'NOT' qualifier are transferred. Putative orthologs are chosen using information combined from a variety of complementary sources. Potential orthologs are initially identified using sequence similarity search programs such as BLAST. Orthology relationships are then verified manually using a combination of resources including sequence analysis tools, phylogenetic and comparative genomics databases such as Ensembl Compara, INPARANOID and OrthoMCL, as well as other specialised databases such as species-specific collections (e.g. HGNC's HCOP). In all cases curators check each alignment and use their experience to assess whether similarity is considered to be strong enough to infer that the two proteins have a common function so that they can confidently project an annotation. While there is no fixed cut-off point in percentage sequence similarity, generally proteins which have greater than 30% identity that covers greater than 80% of the length of both proteins are examined further. For mammalian proteins this cut-off tends to be higher, with an average of 80% identity over 90% of the length of both proteins. Strict orthologs are desirable but not essential. In general, when there is evidence of multiple paralogs for a single species, annotations using less specific GO terms are transferred to the paralogs, however, annotations using more specific GO terms may be transferred to the most similar paralog in each species, this decision is taken on a case by case basis and may be influenced by statements by researchers in the field. Further detailed information on this procedure, including how ISS annotations are made to protein isoforms, can be found at: http://www.ebi.ac.uk/GOA/ISS_method.html.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators.","canto_curator_role":"JaponicusDB","cv_annotations":{"biological_process":[{"annotations":[78547],"is_not":false,"summary":null,"term":"GO:0000122"}],"cellular_component":[{"annotations":[78544],"is_not":false,"summary":null,"term":"GO:0005869"}],"molecular_function":[{"annotations":[78545],"is_not":false,"summary":null,"term":"GO:0001227"},{"annotations":[78546],"is_not":false,"summary":null,"term":"GO:0000978"}]},"gene_count":2,"genes_by_uniquename":{"SJAG_00124":null,"SJAG_01739":null},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{"GO:0000122":null,"GO:0000978":null,"GO:0001227":null,"GO:0005869":null},"title":"Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.","uniquename":"GO_REF:0000024"}


id: GO_REF:0000096
data:
  {"abstract":"Mouse Genome Database (MGD), The HUGO Gene Nomenclature Committee (HGNC), and Rat Genome Database (RGD) have extensive procedures in place, overseen by expert curation, to establish orthology relationships between their genes. The Experimentally based annotations annotated by each group (IDA, IMP IPI, IGI, and EXP) are used to provide annotations  to the respective mouse and rat orthologs, and given the ISO evidence code and an entry in the inferred_from field to indicate the orthologous entity. ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Mouse Genome Informatics scientific curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Automated transfer of experimentally-verified manual GO annotation data to close orthologs.","uniquename":"GO_REF:0000096"}


id: PMID:25308606
data:
  {"abstract":"The non-pathogenic dimorphic fission yeast, Schizosaccharomyces japonicus, could be a suitable model organism for investigation of the genetic background of mycelial growth, as it has a haploid chromosome set and its genome is sequenced. Since earlier results have suggested that its morphological transition required solid substrates, but molecular biological experiments would require hyphae production in a liquid medium, we wanted to find circumstances which would enable hyphae production in liquid media. Several external conditions were investigated, but the strongest inducer was fetal bovine serum (FBS). Its positive effect could be hampered by heat and was dependent on pH, temperature and concentration of the serum. Other protein-containing compounds, such as peptone and bovine serum albumin or amino acids, proved to be ineffective or weak. Generally, the uninduced and induced mycelial growth of Sz. japonicus could be improved by lower external pH and higher temperature.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Papp L, Sipiczki M, Holb IJ, Miklós I","authors_abbrev":"Papp L et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Yeast 2014 Dec;31(12):475-82","cv_annotations":{},"doi":"10.1002/yea.3048","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2014","pubmed_entrez_date":"2014-10-14","pubmed_publication_date":"Dec 2014","terms_by_termid":{},"title":"Optimal conditions for mycelial growth of Schizosaccharomyces japonicus cells in liquid medium: it enables the molecular investigation of dimorphism.","uniquename":"PMID:25308606"}


id: PMID:27697163
data:
  {"abstract":"The present work demonstrates that yeasts belonging to the Schizosaccharomyces genus release a high quantity of polysaccharides of cell wall origin starting from the onset of the alcoholic fermentation. By the end of the alcoholic fermentation, all of the Schizosaccharomyces yeast strains released a quantity of polysaccharides approximately 3-7 times higher than that released by a commercial Saccharomyces cerevisiae yeast strain under the same fermentative conditions of synthetic juice. A higher content of polysaccharide was found in media fermented by Schizosaccharomyces japonicus with respect to that of Schizosaccharomyces pombe. Some of the strains evaluated were also able to produce high levels of pyruvic acid, which has been shown to be an important compound for color stability of wine. The presence of strains with different malic acid consumption patterns along with high polysaccharide release would enable production of naturally modified wines with enhanced mouth feel and reduced acidity. The chemical analysis of the released polysaccharides demonstrated divergence between the two yeast species S. pombe and S. japonicus. A different mannose/galactose ratio and a different percentage of proteins was observed on the polysaccharides released by S. pombe as compared to S. japonicus. Analysis of the proteins released in the media revealed the presence of a glycoprotein with a molecular size around 32-33 kDa only for the species S. japonicus. Mass spectrometry analysis of carbohydrate moieties showed similar proportions among the N-glycan chains released in the media by both yeast species but differences between the two species were also observed. These observations suggest a possible role of rapid MALDI-TOF screening of N-glycans compositional fingerprint as a taxonomic tool for this genus. Polysaccharides release in the media, in particular galactomannoproteins in significant amounts, could make these yeasts particularly interesting also for the industrial production of exogenous polysaccharide preparations.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Domizio P, Liu Y, Bisson LF, Barile D","authors_abbrev":"Domizio P et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Food Microbiol 2017 Feb;61:136-149","cv_annotations":{},"doi":"10.1016/j.fm.2016.08.010","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2016-10-05","pubmed_publication_date":"Feb 2017","terms_by_termid":{},"title":"Cell wall polysaccharides released during the alcoholic fermentation by Schizosaccharomyces pombe and S. japonicus: quantification and characterization.","uniquename":"PMID:27697163"}


id: GO_REF:0000002
data:
  {"abstract":"Transitive assignment of GO terms based on InterPro classification. For any database entry (representing a protein or protein-coding gene) that has been annotated with one or more InterPro domains, the corresponding GO terms are obtained from a translation table of InterPro entries to GO terms (interpro2go) generated manually by the InterPro team at EBI. The mapping file is available at http://www.geneontology.org/external2go/interpro2go.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"DDB, FB, MGI, GOA, ZFIN 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id: PMID:32265131
data:
  {"abstract":"The N- and O-linked oligosaccharides from fission yeast Schizosaccharomyces pombe not only contain large amounts of d-mannose (Man) but also contain large amounts of d-galactose (Gal). Although the galactomannans of S. pombe are mainly composed of α1,2- or α1,3-linked Gals, some of the terminal α1,2-linked Gals are found to be linked to pyruvylated β1,3-linked galactose (PvGal). We have determined the structural characteristics of the N-glycans and O-glycans in three Schizosaccharomyces species (S. japonicus, S. octosporus, and S. cryophilus) using lectin blot,  1 H NMR spectroscopy, and size-fractionation high performance liquid chromatography (HPLC), and found that the galactosylation of oligosaccharides was a common feature in fission yeasts. In addition, each of the terminal Galα1,2-, Galβ1,3- and non-substituted Man residues exhibited distinct characteristics. A BLAST search of gene databases in Schizosaccharomyces identified genes homologous to pvg1 encoding pyruvyltransferase of S. pombe. These genes, when expressed in an S. pombe pvg1Δ strains, led to the pyruvylation of non-reducing terminal β-linked Gal, suggesting the biosynthetic pathway of PvGal-containing oligosaccharides is highly conserved in fission yeasts.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Fukunaga T, Tanaka N, Furumoto T, Nakakita S, Ohashi T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Fukunaga T et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Biosci Bioeng 2020 Aug;130(2):128-136","cv_annotations":{},"doi":"10.1016/j.jbiosc.2020.03.008","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2020","pubmed_entrez_date":"2020-04-09","pubmed_publication_date":"Aug 2020","terms_by_termid":{},"title":"Characterization of N- and O-linked galactosylated oligosaccharides from fission yeast species.","uniquename":"PMID:32265131"}


id: PMID:28733395
data:
  {"abstract":" Schizosaccharomyces japonicus  is a dimorphic yeast. Depending on the nutrient conditions, the transition between growth as yeast cells and growth as hyphal cells can be reversibly induced. In addition to nutrient stress, induced DNA lesions, such as those produced by camptothecin, also induce hyphal growth regardless of the nutrient status. This protocol describes both methods of induction.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Niki H","authors_abbrev":"Niki H","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Cold Spring Harb Protoc 2017 Dec 01;2017(12):pdb.prot091868","cv_annotations":{},"doi":"10.1101/pdb.prot091868","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2017-07-23","pubmed_publication_date":"01 Dec 2017","terms_by_termid":{},"title":"Induction of Hyphal Growth in  Schizosaccharomyces japonicus .","uniquename":"PMID:28733395"}


id: GO_REF:0000021
data:
  {"abstract":"Current genetic and molecular studies in many model organisms are aimed at understanding formation and development of the nervous system. Up until this point, the GO has had a very shallow representation of processes pertaining to the nervous system. In June 2006, curators from MGI and ZFIN met with researchers studying central nervous system development to improve the representation of these processes in GO. In particular, emphasis was placed on three areas that are being addressed actively in current research: forebrain development, hindbrain development and neural tube development. This collaboration resulted in the addition of over 500 terms that reflect the development of the forebrain, the hindbrain, and the neural tube from the perspective of biological process and anatomical structure.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Judith Blake (1, 2), William Bug (3), Rex Chisholm (1, 4), Jennifer Clark (1, 5), Erika Feltrin (6), Jacqueline Finger (2), David Hill (1, 2), Midori Harris (1, 5), Terry Hayamizu (2), Doug Howe (9), Maryanne Martone (7), Kathleen Millen (8), Francis Sele (4) (1. The Gene Ontology Consortium, 2. Mouse Genome Informatics, Bar Harbor, ME, 3. Drexel University, Philadelphia, PA, 4. Northwestern University, Chicago, IL, 5. EMBL-EBI, Hinxton, Cambridgeshire, UK, 6. The University of Padua, Padua, Italy, 7. The University of California at San Diego, San Diego, CA, 8. The University of Chicago, Chicago, IL, 9. The Zebrafish Information Network, University of Oregon, Eugene, OR)","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Improving the representation of central nervous system development in the biological process ontology","uniquename":"GO_REF:0000021"}


id: GO_REF:0000087
data:
  {"abstract":"We have created a standard template for classes describing the protein localization and establishment of protein localization to a cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0008104 and 'has_target_end_location' some C\" (protein localization) and \"GO:0045184 and 'has_target_end_location' some C\" (establishment of protein localization), where C is cellular component.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of protein localization and establishment of protein localization as biological process in the Gene Ontology","uniquename":"GO_REF:0000087"}


id: PMID:8529460
data:
  {"abstract":"Meiotic prophase in Schizosaccharomyces pombe is characterized by striking nuclear movements and the formation of linear elements along chromosomes instead of tripartite synaptonemal complexes. We analysed the organization of nuclei and microtubules in cells of fission yeasts undergoing sexual differentiation. S. japonicus var. versatilis and S. pombe cells were studied in parallel, taking advantage of the better cytology in S. versatilis. During conjugation, microtubules were directed towards the mating projection. These microtubules seem to lead the haploid nuclei together in the zygote by interaction with the spindle pole bodies at the nuclear periphery. After karyogamy, arrays of microtubules emanating from the spindle pole body of the diploid nucleus extended to both cell poles. The same differentiated microtubule configuration was elaborated upon induction of azygotic meiosis in S. pombe. The cyclic movements of the elongated nuclei between the cell poles is reflected by a dynamic and coordinated shortening and lengthening of the two microtubule arrays. When the nucleus was at a cell end, one array was short while the other bridged the whole cell length. Experiments with inhibitors showed that microtubules are required for karyogamy and for the elongated shape and movement of nuclei during meiotic prophase. In both fission yeasts the SPBs and nucleoli are at the leading ends of the moving nuclei. Astral and cytoplasmic microtubules were also prominent during meiotic divisions and sporulation. We further show that in S. versatilis the linear elements formed during meiotic prophase are similar to those in S. pombe. Tripartite synaptonemal complexes were never detected. Taken together, these findings suggest that S. pombe and S. versatilis share basic characteristics in the organization of microtubules and the structure and behaviour of nuclei during their meiotic cell cycle. The prominent differentiations of microtubules and nuclei may be involved in the pairing, recombination, and segregation of meiotic chromosomes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Svoboda A, Bähler J, Kohli J","authors_abbrev":"Svoboda A et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Chromosoma 1995 Nov;104(3):203-14","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1995","pubmed_entrez_date":"1995-11-01","pubmed_publication_date":"Nov 1995","terms_by_termid":{},"title":"Microtubule-driven nuclear movements and linear elements as meiosis-specific characteristics of the fission yeasts Schizosaccharomyces versatilis and Schizosaccharomyces pombe.","uniquename":"PMID:8529460"}


id: PMID:26343758
data:
  {"abstract":"CENP-A is a centromere-specific histone H3 variant that is required for kinetochore assembly and accurate chromosome segregation. For it to function properly, CENP-A must be specifically localized to centromeres. In fission yeast, Scm3sp and the Mis18 complex, composed of Mis16, Eic1, and Mis18, function as a CENP-A(Cnp1)-specific chaperone and a recruiting factor, respectively, and together ensure accurate delivery of CENP-A(Cnp1) to centromeres. Although how Scm3sp specifically recognizes CENP-A(Cnp1) has been revealed recently, the recruiting mechanism of CENP-A(Cnp1) via the Mis18 complex remains unknown. In this study, we have determined crystal structures of Schizosaccharomyces japonicus Mis16 alone and in complex with the helix 1 of histone H4 (H4α1). Crystal structures followed by mutant analysis and affinity pull-downs have revealed that Mis16 recognizes both H4α1 and Scm3sp independently within the CENP-A(Cnp1)/H4:Scm3sp complex. This observation suggests that Mis16 gains CENP-A(Cnp1) specificity by recognizing both Scm3sp and histone H4. Our studies provide insights into the molecular mechanisms underlying specific recruitment of CENP-A(Cnp1)/H4:Scm3sp into centromeres. ","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":4,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-05-13","authors":"An S, Kim H, Cho US","authors_abbrev":"An S et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-05-13 14:11:41","canto_curator_name":"Val Wood","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-05-13 14:11:41","canto_session_key":"fb189c5ef542852c","canto_session_submitted_date":"2021-05-12 16:00:22","canto_triage_status":"Curatable","citation":"J Mol Biol 2015 Oct 09;427(20):3230-3240","cv_annotations":{"molecular_function":[{"annotations":[115222,115223,115224,115225],"is_not":false,"summary":null,"term":"GO:0042393"}]},"doi":"10.1016/j.jmb.2015.08.022","gene_count":4,"genes_by_uniquename":{"SJAG_00303":null,"SJAG_02513":null,"SJAG_03542":null,"SJAG_03867":null},"genotypes_by_uniquename":{},"ltp_gene_count":3,"ortholog_annotations":[],"paralog_annotations":[],"pdb_entries":[{"entry_authors":"An S,Kim H,Cho U-S","entry_authors_abbrev":"An S et al.","experimental_method":"X-ray","gene_chains":[{"chain":"B","gene_uniquename":"SJAG_03542","position":"1-103"},{"chain":"A","gene_uniquename":"SJAG_03867","position":"1-427"}],"pdb_id":"4xyi","reference_uniquename":"PMID:26343758","resolution":"3.0","title":"Mis16 with H4 peptide"},{"entry_authors":"An S,Kim H,Cho U-S","entry_authors_abbrev":"An S et al.","experimental_method":"X-ray","gene_chains":[{"chain":"A","gene_uniquename":"SJAG_03867","position":"1-427"}],"pdb_id":"4xyh","reference_uniquename":"PMID:26343758","resolution":"2.3","title":"Wild-type full length Mis16 in Schizosaccharomyces japonicus"}],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-09-08","pubmed_publication_date":"09 Oct 2015","terms_by_termid":{"GO:0042393":null},"title":"Mis16 Independently Recognizes Histone H4 and the CENP-ACnp1-Specific Chaperone Scm3sp.","uniquename":"PMID:26343758"}


id: GO_REF:0000012
data:
  {"abstract":"Pairwise alignments are generated by taking two sequences and aligning them so that the maximum number of amino acids in each protein match, or are similar to, each other. Tools such as BLAST work by comparing a protein-of-interest individually with every protein in a database of known protein sequences and retaining only those matches with a high probability of being significant. Basic BLAST generates local alignments between proteins for regions of high similarity. Other pairwise alignment tools attempt to generate global (full-length) protein alignments. A tool called Blast_Extend_repraze (BER, http://ber.sourceforge.net) has some benefits over basic BLAST. Input into the BER tool includes the underlying DNA sequence for each protein as well as 300 nucleotides upstream and downstream of the predicted boundaries of the protein coding sequence. This allows annotators to see the DNA sequence that underlies the query protein as part of the alignment. In addition, the BER tool is able to look for continuation of regions of similarity through frameshifts and in-frame stop codons.  If such regions are found the alignment is continued. BER searches are done in a two-step process: step one is a BLAST search against a non-redundant protein database, significant BLAST hits are stored in a mini-database for each query protein; step two is a modified Smith-Waterman alignment between the query and the proteins in its mini-database. In order to assess whether a given BER alignment is good enough to assert that the query shares the function of the match protein, one must look at a several factors. First of all, the match protein must itself be experimentally characterized in order to avoid transitive annotation errors. In addition, any residues or secondary structures known to be important for function in the match protein must be conserved in the query. The alignment should be visually inspected to look for any areas of lesser quality that might indicate the two proteins do not share the same function. Although it is impossible to set cutoff values for percent identity and length of match that will apply for every alignment, there are some guidelines. In general at least 40% identity that extends over the full lengths of both proteins is required in order to even consider functional equivalence. However, this percentage is highly dependent on the length and complexity of the proteins. 40% identity between two proteins 500 amino acids long is much more significant that 40% identity between two proteins that are only 100 amino acids long. Therefore, the annotator's experience and knowledge of what is considered significant for the organism and protein family in question is very important. Some sets of proteins are much more highly conserved than others and therefore tolerances for percent identity may have to be adjusted. Finally, the alignment must be considered in the context of what else is known about the query protein and the organism as a whole.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Michelle Gwinn, TIGR curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Pairwise alignment (TIGR)","uniquename":"GO_REF:0000012"}


id: PMID:23090706
data:
  {"abstract":"DNA damage response includes DNA repair, nucleotide metabolism and even a control of cell fates including differentiation, cell death pathway or some combination of these. The responses to DNA damage differ from species to species. Here we aim to delineate the checkpoint pathway in the dimorphic fission yeast Schizosaccharomyces japonicus, where DNA damage can trigger a differentiation pathway that is a switch from a bidirectional yeast growth mode to an apical hyphal growth mode, and the switching is regulated via a checkpoint kinase, Chk1. This Chk1-dependent switch to hyphal growth is activated with even low doses of agents that damage DNA; therefore, we reasoned that this switch may depend on other genes orthologous to the components of the classical Sz. pombe Chk1-dependent DNA checkpoint pathway. As an initial test of this hypothesis, we assessed the effects of mutations in Sz. japonicus orthologs of Sz. pombe checkpoint genes on this switch from bidirectional to hyphal growth. The same set of DNA checkpoint genes was confirmed in Sz. japonicus. We tested the effect of each DNA checkpoint mutants on hyphal differentiation by DNA damage. We found that the Sz. japonicus hyphal differentiation pathway was dependent on Sz. japonicus orthologs of Sz. pombe checkpoint genes-(SP)rad3, (SP)rad26, (SP)rad9, (SP)rad1, (SP)rad24, (SP)rad25, (SP)crb2, and (SP)chk1-that function in the DNA damage checkpoint pathway, but was not dependent on orthologs of two Sz. pombe genes-(SP)cds1 or (SP)mrc1-that function in the DNA replication checkpoint pathway. These findings indicated that although the role of each component of the DNA damage checkpoint and DNA replication checkpoint is mostly same between the two fission yeasts, the DNA damage checkpoint was the only pathway that governed DNA damage-dependent hyphal growth. We also examined whether DNA damage checkpoint signaling engaged in functional crosstalk with other hyphal differentiation pathways because hyphal differentiation can also be triggered by nutritional stress. Here, we discovered genetic interactions that indicated that the cAMP pathway engaged in crosstalk with Chk1-dependent signaling.","alleles_by_uniquename":{"SJAG_00364:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00364","name":"rad3delta","uniquename":"SJAG_00364:allele-1"},"SJAG_00429:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00429","name":"rad26delta","uniquename":"SJAG_00429:allele-1"},"SJAG_01205:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01205","name":"crb2delta","uniquename":"SJAG_01205:allele-1"},"SJAG_01605:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01605","name":"rad9delta","uniquename":"SJAG_01605:allele-1"},"SJAG_01680:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01680","name":"chk1delta","uniquename":"SJAG_01680:allele-1"},"SJAG_01680:allele-2":{"allele_type":"amino_acid_mutation","description":"P470L","gene_uniquename":"SJAG_01680","name":"chk1-P470L","synonyms":[{"name":"chk1- hyperactive (chk1-hyp)","reference":"PMID:23090706","type":"exact"},{"name":"chk1-hyperactive (chk1-hyp)","reference":"PMID:20368354","type":"exact"}],"uniquename":"SJAG_01680:allele-2"},"SJAG_02266:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02266","name":"rad24delta","uniquename":"SJAG_02266:allele-1"},"SJAG_02576:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02576","name":"rad25delta","uniquename":"SJAG_02576:allele-1"},"SJAG_02771:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02771","name":"rad1delta","uniquename":"SJAG_02771:allele-1"},"SJAG_03720:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03720","name":"tel1delta","uniquename":"SJAG_03720:allele-1"},"SJAG_04287:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04287","name":"cds1delta","uniquename":"SJAG_04287:allele-1"},"SJAG_04671:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04671","name":"mrc1delta","uniquename":"SJAG_04671:allele-1"}},"annotation_curators":[{"annotation_count":28,"community_curator":true,"file_name":null,"file_type":null,"name":"Sho Okamoto","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-11-21","authors":"Furuya K, Niki H","authors_abbrev":"Furuya K et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2022-11-21 17:21:20","canto_curator_name":"Sho Okamoto","canto_curator_role":"community","canto_first_approved_date":"2022-11-21 17:21:20","canto_session_key":"5f68f94ee65a99b7","canto_session_submitted_date":"2022-11-21 17:21:13","canto_triage_status":"Curatable","citation":"Curr Genet 2012 Dec;58(5-6):291-303","cv_annotations":{"multi_locus_phenotype":[{"annotations":[115546],"is_not":false,"summary":null,"term":"FYPO:0007790"},{"annotations":[115552],"is_not":false,"summary":null,"term":"FYPO:0000085"},{"annotations":[115549],"is_not":false,"summary":null,"term":"FYPO:0000088"}],"single_locus_phenotype":[{"annotations":[115537,115538,115539,115540,115541,115542,115544,115545],"is_not":false,"summary":null,"term":"FYPO:0007782"},{"annotations":[115563],"is_not":false,"summary":null,"term":"FYPO:0007774"},{"annotations":[115562],"is_not":false,"summary":null,"term":"FYPO:0001690"},{"annotations":[115536,115543],"is_not":false,"summary":null,"term":"FYPO:0007790"},{"annotations":[115561],"is_not":false,"summary":null,"term":"FYPO:0004693"},{"annotations":[115550,115551,115556,115557,115558],"is_not":false,"summary":null,"term":"FYPO:0000085"},{"annotations":[115547,115548,115553,115554,115555],"is_not":false,"summary":null,"term":"FYPO:0000088"},{"annotations":[115559,115560],"is_not":false,"summary":null,"term":"FYPO:0001234"}]},"doi":"10.1007/s00294-012-0384-4","gene_count":11,"genes_by_uniquename":{"SJAG_00364":null,"SJAG_00429":null,"SJAG_01205":null,"SJAG_01605":null,"SJAG_01680":null,"SJAG_02266":null,"SJAG_02576":null,"SJAG_02771":null,"SJAG_03720":null,"SJAG_04287":null,"SJAG_04671":null},"genotypes_by_uniquename":{"cds1delta":{"display_name":"cds1delta","display_uniquename":"cds1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04287:allele-1","expression":"Null"}]}]},"chk1-P470L-P470L-amino_acid_mutation-expression-not_assayed_or_wild_type__rad24delta":{"display_name":"chk1-P470L(aa) rad24delta","display_uniquename":"chk1-P470L-P470L-amino_acid_mutation-expression-not_assayed_or_wild_type__rad24delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01680:allele-2","expression":"Not assayed or wild type"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_02266:allele-1","expression":"Null"}]}]},"chk1delta":{"display_name":"chk1delta","display_uniquename":"chk1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01680:allele-1","expression":"Null"}]}]},"chk1delta__crb2delta":{"display_name":"chk1delta crb2delta","display_uniquename":"chk1delta__crb2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01680:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_01205:allele-1","expression":"Null"}]}]},"crb2delta":{"display_name":"crb2delta","display_uniquename":"crb2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01205:allele-1","expression":"Null"}]}]},"mrc1delta":{"display_name":"mrc1delta","display_uniquename":"mrc1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04671:allele-1","expression":"Null"}]}]},"rad1delta":{"display_name":"rad1delta","display_uniquename":"rad1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02771:allele-1","expression":"Null"}]}]},"rad24delta":{"display_name":"rad24delta","display_uniquename":"rad24delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02266:allele-1","expression":"Null"}]}]},"rad25delta":{"display_name":"rad25delta","display_uniquename":"rad25delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02576:allele-1","expression":"Null"}]}]},"rad26delta":{"display_name":"rad26delta","display_uniquename":"rad26delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00429:allele-1","expression":"Null"}]}]},"rad3delta":{"display_name":"rad3delta","display_uniquename":"rad3delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00364:allele-1","expression":"Null"}]}]},"rad9delta":{"display_name":"rad9delta","display_uniquename":"rad9delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01605:allele-1","expression":"Null"}]}]},"tel1delta":{"display_name":"tel1delta","display_uniquename":"tel1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03720:allele-1","expression":"Null"}]}]}},"ltp_gene_count":11,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2012","pubmed_entrez_date":"2012-10-24","pubmed_publication_date":"Dec 2012","references_by_uniquename":{"PMID:20368354":null,"PMID:23090706":null},"terms_by_termid":{"FYECO:0000005":null,"FYECO:0000137":null,"FYECO:0000314":null,"FYPO:0000085":null,"FYPO:0000088":null,"FYPO:0001234":null,"FYPO:0001690":null,"FYPO:0004693":null,"FYPO:0007774":null,"FYPO:0007782":null,"FYPO:0007790":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null},"title":"Hyphal differentiation induced via a DNA damage checkpoint-dependent pathway engaged in crosstalk with nutrient stress signaling in Schizosaccharomyces japonicus.","uniquename":"PMID:23090706"}


id: GO_REF:0000068
data:
  {"abstract":"We have created a standard template for classes each describing the metabolism, catabolism, or biosynthesis of a chemical entity (ChEBI) as a process. The underlying equivalence axiom templates are \"GO:0008152 and 'has participant' some X\" (metabolism), \"GO:0009056 and 'has input' some X\" (catabolism), \"GO:0009058 and 'has output' some X\" and (biosynthesis),  where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of metabolic triad (metabolism, catabolism, biosynthesis) as biological process in the Gene Ontology","uniquename":"GO_REF:0000068"}


id: PMID:35226668
data:
  {"abstract":"RNA interference (RNAi) is a conserved mechanism of small RNA-mediated genome regulation commonly involved in suppression of transposable elements (TEs) through both post-transcriptional silencing, and transcriptional repression via heterochromatin assembly. The fission yeast Schizosaccharomyces pombe has been extensively utilised as a model for studying RNAi pathways. However, this species is somewhat atypical in that TEs are not major targets of RNAi, and instead small RNAs correspond primarily to non-coding pericentromeric repeat sequences, reflecting a specialised role for the pathway in promoting heterochromatin assembly in these regions. In contrast, in the related fission yeast Schizosaccharomyces japonicus, sequenced small RNAs correspond primarily to TEs. This suggests there may be fundamental differences in the operation of RNAi pathways in these two related species. To investigate these differences, we probed RNAi function in S. japonicus. Unexpectedly, and in contrast to S. pombe, we found that RNAi is essential in this species. Moreover, viability of RNAi mutants can be rescued by mutations implicated in enhancing RNAi-independent heterochromatin propagation. These rescued strains retain heterochromatic marks on TE sequences, but exhibit derepression of TEs at the post-transcriptional level. Our findings indicate that S. japonicus retains the ancestral role of RNAi in facilitating suppression of TEs via both post-transcriptional silencing and heterochromatin assembly, with specifically the heterochromatin pathway being essential for viability, likely due to a function in genome maintenance. The specialised role of RNAi in heterochromatin assembly in S. pombe appears to be a derived state that emerged after the divergence of S. japonicus.","alleles_by_uniquename":{"SJAG_02409:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02409","name":"stc1delta","uniquename":"SJAG_02409:allele-1"},"SJAG_02594:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02594","name":"arb1delta","uniquename":"SJAG_02594:allele-1"},"SJAG_02621:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02621","name":"ago1delta","uniquename":"SJAG_02621:allele-1"},"SJAG_02668:allele-1":{"allele_type":"amino_acid_mutation","description":"R77W","gene_uniquename":"SJAG_02668","name":"mpe1-R77W","uniquename":"SJAG_02668:allele-1"},"SJAG_03118:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03118","name":"leo1delta","uniquename":"SJAG_03118:allele-1"},"SJAG_03118:allele-2":{"allele_type":"nonsense_mutation","description":"aa61->stop","gene_uniquename":"SJAG_03118","name":"frameshift","uniquename":"SJAG_03118:allele-2"},"SJAG_03356:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03356","name":"rdp1delta","uniquename":"SJAG_03356:allele-1"},"SJAG_03689:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03689","name":"dcr1delta","uniquename":"SJAG_03689:allele-1"},"SJAG_03916:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03916","name":"chp1delta","uniquename":"SJAG_03916:allele-1"},"SJAG_04061:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04061","name":"arb2delta","uniquename":"SJAG_04061:allele-1"},"SJAG_04574:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04574","name":"clr4delta","uniquename":"SJAG_04574:allele-1"}},"annotation_curators":[{"annotation_count":31,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-03-07","authors":"Chapman E, Taglini F, Bayne EH","authors_abbrev":"Chapman E et al.","canto_added_date":"2022-03-07 09:13:19","canto_annotation_status":"APPROVED","canto_approved_date":"2022-03-07 12:35:06","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2022-03-07 12:35:06","canto_session_key":"3d6467bf1cb92446","canto_session_submitted_date":"2022-03-07 12:34:56","canto_triage_status":"Curatable","citation":"PLoS Genet 2022 Feb 28;18(2):e1010100","cv_annotations":{"biological_process":[{"annotations":[115390,115391],"is_not":false,"summary":null,"term":"GO:0031507"},{"annotations":[115388,115389],"is_not":false,"summary":null,"term":"GO:0016441"}],"multi_locus_phenotype":[{"annotations":[115384,115386],"is_not":false,"summary":null,"term":"FYPO:0004982"},{"annotations":[115385,115387],"is_not":false,"summary":null,"term":"FYPO:0004573"},{"annotations":[115381],"is_not":false,"summary":null,"term":"FYPO:0002061"},{"annotations":[115382,115383],"is_not":false,"summary":null,"term":"FYPO:0006989"},{"annotations":[115376,115377,115378,115379],"is_not":false,"summary":null,"term":"FYPO:0002058"}],"single_locus_phenotype":[{"annotations":[115370],"is_not":false,"summary":null,"term":"FYPO:0004205"},{"annotations":[115372],"is_not":false,"summary":null,"term":"FYPO:0004982"},{"annotations":[115374],"is_not":false,"summary":null,"term":"FYPO:0000595"},{"annotations":[115371],"is_not":false,"summary":null,"term":"FYPO:0004574"},{"annotations":[115363,115364,115365,115366,115367,115368,115369,115380],"is_not":false,"summary":null,"term":"FYPO:0002061"},{"annotations":[115375],"is_not":false,"summary":null,"term":"FYPO:0006989"},{"annotations":[115373],"is_not":false,"summary":null,"term":"FYPO:0000596"}]},"doi":"10.1371/journal.pgen.1010100","gene_count":10,"genes_by_uniquename":{"SJAG_02409":null,"SJAG_02594":null,"SJAG_02621":null,"SJAG_02668":null,"SJAG_03118":null,"SJAG_03356":null,"SJAG_03689":null,"SJAG_03916":null,"SJAG_04061":null,"SJAG_04574":null},"genetic_interactions":[[{"gene_a_uniquename":"SJAG_03689","gene_b_uniquename":"SJAG_03118","interaction_type":"Phenotypic Suppression"},[{"reference_uniquename":"PMID:35226668","throughput":"low"}]],[{"gene_a_uniquename":"SJAG_03689","gene_b_uniquename":"SJAG_02668","interaction_type":"Phenotypic Suppression"},[{"reference_uniquename":"PMID:35226668","throughput":"low"}]]],"genotypes_by_uniquename":{"ago1delta":{"display_name":"ago1delta","display_uniquename":"ago1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02621:allele-1","expression":"Null"}]}]},"ago1delta__leo1delta":{"display_name":"ago1delta leo1delta","display_uniquename":"ago1delta__leo1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02621:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03118:allele-1","expression":"Null"}]}]},"arb1delta":{"display_name":"arb1delta","display_uniquename":"arb1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02594:allele-1","expression":"Null"}]}]},"arb2delta":{"display_name":"arb2delta","display_uniquename":"arb2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04061:allele-1","expression":"Null"}]}]},"chp1delta":{"display_name":"chp1delta","display_uniquename":"chp1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03916:allele-1","expression":"Null"}]}]},"clr4delta":{"display_name":"clr4delta","display_uniquename":"clr4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04574:allele-1","expression":"Null"}]}]},"clr4delta__leo1delta":{"display_name":"clr4delta leo1delta","display_uniquename":"clr4delta__leo1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04574:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03118:allele-1","expression":"Null"}]}]},"dcr1delta":{"display_name":"dcr1delta","display_uniquename":"dcr1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03689:allele-1","expression":"Null"}]}]},"dcr1delta__frameshift-aa61->stop-nonsense_mutation-expression-not_assayed_or_wild_type":{"display_name":"dcr1delta frameshift(aa61->stop)","display_uniquename":"dcr1delta__frameshift-aa61->stop-nonsense_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03689:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03118:allele-2","expression":"Not assayed or wild type"}]}]},"dcr1delta__leo1delta":{"display_name":"dcr1delta leo1delta","display_uniquename":"dcr1delta__leo1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03689:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03118:allele-1","expression":"Null"}]}]},"dcr1delta__mpe1-R77W-R77W-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"dcr1delta mpe1-R77W(aa)","display_uniquename":"dcr1delta__mpe1-R77W-R77W-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03689:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_02668:allele-1","expression":"Not assayed or wild type"}]}]},"rdp1delta":{"display_name":"rdp1delta","display_uniquename":"rdp1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03356:allele-1","expression":"Null"}]}]},"stc1delta":{"display_name":"stc1delta","display_uniquename":"stc1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02409:allele-1","expression":"Null"}]}]}},"ltp_gene_count":10,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-02-28","pubmed_publication_date":"28 Feb 2022","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000162":null,"FYPO:0000595":null,"FYPO:0000596":null,"FYPO:0002058":null,"FYPO:0002061":null,"FYPO:0004205":null,"FYPO:0004573":null,"FYPO:0004574":null,"FYPO:0004982":null,"FYPO:0006989":null,"FYPO_EXT:0000001":null,"GO:0016441":null,"GO:0031507":null},"title":"Separable roles for RNAi in regulation of transposable elements and viability in the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:35226668"}


id: GO_REF:0000097
data:
  {"abstract":"FlyBase occasionally makes GO annotations based on information that has been sent to us directly by researchers as a personal communication to FlyBase. In each case, the full details of the communication including any associated data and analyses are recorded in a FlyBase publication (FBrf) available from our website (http://flybase.org).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"FlyBase","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Gene Ontology annotation based on personal communication to FlyBase","uniquename":"GO_REF:0000097"}


id: GO_REF:0000085
data:
  {"abstract":"We have created a standard template for classes describing the apoptotic process for a cell type as a biological process. The underlying equivalence axiom template is \"'apoptotic process' and 'occurs in' some C\", where C is a native cell (CL:0000003).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of cell apoptotic process as biological process in the Gene Ontology","uniquename":"GO_REF:0000085"}


id: GO_REF:0000063
data:
  {"abstract":"We have created a standard template for classes describing processes regulated by other regulating processes. The underlying equivalence axiom template is \"R and 'results_in' some P\", where R is a biological process and P is a regulation of biological process subclass.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of processes regulated by other regulating processes in the Gene Ontology","uniquename":"GO_REF:0000063"}


id: PMID:27678009
data:
  {"abstract":"The cAMP cascade plays an important role in several biological processes. Thus, study of its molecular details can contribute to a better understanding of these processes, treatment of diseases, or even finding antifungal drug targets. To gain further information about the PKA pathway, and its evolutionarily conserved and species-specific features, the central regulator pka1 gene, which encodes the cAMP-dependent protein kinase catalytic subunit, was studied in the less known haplontic, dimorphic fission yeast Schizosaccharomyces japonicus. Namely, this species belongs to a highly divergent phylogenetic branch of fungi. Furthermore, S. japonicus had only a single copy pka1 gene in contrast to the budding yeasts. Therefore, the pka1 deleted mutant was created, whose RNA sequencing and phenotypic studies revealed that the Pka1 regulated at least 373 genes, among them further kinases, phosphatases and transcriptional regulators. It regulated elongation of hyphae, cell size, aging and stress response. Furthermore, half of the pka1 target genes seemed to be conserved in Schizosaccharomyces pombe and S. japonicus. However, there were oppositely regulated genes in the two closely related species. The target genes suggest that this single gene must be able to fulfill all the functions of TPK1-3 of Saccharomyces cerevisiae. Thus, our results shed light on certain similarities and differences of the PKA pathway of S. japonicus compared to the budding yeasts and confirmed the multifunctionality of the pka1 gene, but further experiments are needed to prove its involvement in the metabolic processes and transport.","alleles_by_uniquename":{"SJAG_04312:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04312","name":"pka1delta","uniquename":"SJAG_04312:allele-1"}},"annotation_curators":[{"annotation_count":6,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-07","authors":"Papp L, Sipiczki M, Miklós I","authors_abbrev":"Papp L et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-07-07 12:57:27","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-07 12:57:27","canto_session_key":"9dc3302039d46818","canto_session_submitted_date":"2021-07-07 12:56:39","canto_triage_status":"Curatable","citation":"Curr Genet 2017 Jun;63(3):487-497","cv_annotations":{"single_locus_phenotype":[{"annotations":[115531],"is_not":false,"summary":null,"term":"FYPO:0007773"},{"annotations":[115530],"is_not":false,"summary":null,"term":"FYPO:0001122"},{"annotations":[115532],"is_not":false,"summary":null,"term":"FYPO:0000245"},{"annotations":[115534],"is_not":false,"summary":null,"term":"FYPO:0000097"},{"annotations":[115533],"is_not":false,"summary":null,"term":"FYPO:0000087"},{"annotations":[115535],"is_not":false,"summary":null,"term":"FYPO:0001214"}]},"doi":"10.1007/s00294-016-0651-x","gene_count":1,"genes_by_uniquename":{"SJAG_04312":null},"genotypes_by_uniquename":{"pka1delta":{"display_name":"pka1delta","display_uniquename":"pka1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04312:allele-1","expression":"Null"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2016-09-29","pubmed_publication_date":"Jun 2017","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000005":null,"FYECO:0000102":null,"FYECO:0000137":null,"FYPO:0000087":null,"FYPO:0000097":null,"FYPO:0000245":null,"FYPO:0001122":null,"FYPO:0001214":null,"FYPO:0007773":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null},"title":"Expression pattern and phenotypic characterization of the mutant strain reveals target genes and processes regulated by pka1 in the dimorphic fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:27678009"}


id: PMID:8546451
data:
  {"abstract":"The phylogenesis of fungi is controversial due to their simple morphology and poor fossilization. Traditional classification supported by morphological studies and physiological traits placed the fission yeasts in one group with ascomycetous yeasts. The rRNA sequence comparisons, however, revealed an enormous evolutionary gap between Saccharomyces and Schizosaccharomyces. As shown in this review, the protein sequences also show a large gap which is almost as large as that separating Schizosaccharomyces from higher animals. Since the two yeasts share features (both cytological and molecular) in common which are also characteristic of ascomycetous fungi, their separation must have taken place later than the sequence differences may suggest. Possible reasons for the paradox are discussed. The sequence data also suggest a slower evolutionary rate in the Schizosaccharomyces lineage than in the Saccharomyces branch. In the fission yeast lineage two ramifications can be supposed. First S. japonicus (Hasegawaea japonica) branched off, then S. octosporus (Octosporomyces octosporus) separated from S. pombe.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Sipiczki M","authors_abbrev":"Sipiczki M","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Phylogeny and evolutionary studies","citation":"Antonie Van Leeuwenhoek 1995 Aug;68(2):119-49","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1995","pubmed_entrez_date":"1995-08-01","pubmed_publication_date":"Aug 1995","terms_by_termid":{},"title":"Phylogenesis of fission yeasts. Contradictions surrounding the origin of a century old genus.","uniquename":"PMID:8546451"}


id: GO_REF:0000090
data:
  {"abstract":"We have created a rule-based approach to create relations between the branches of the Gene Ontology. The approach uses the equivalence axioms and a given pattern to create non-subClassOf relationships between the three different branches of the Gene Ontology (biological process, molecular function, cellular component). Currently, there are the following rules: \"'transporter activity' and 'transports_or_maintains_localization_of' some X' -part_of-> \"transport and 'transports_or_maintains_localization_of' some X\"; \"'transmembrane transporter activity' and 'transports_or_maintains_localization_of' some X -part_of-> 'transmembrane transport' and 'transports_or_maintains_localization_of' some X\"","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Automatic creation of relationships between ontology branches in the Gene Ontology","uniquename":"GO_REF:0000090"}


id: PMID:37849458
data:
  {"abstract":"We previously demonstrated that we could hijack the fungal pheromone signaling pathway to provide a living yeast biosensor where peptide biomarkers were recognized by G-protein-coupled receptors and engineered to transcribe a readout. Here, we demonstrated that the protease could be reintroduced to the biosensor to provide a simple mechanism for distinguishing single-amino-acid changes in peptide ligands that, otherwise, would likely be difficult to detect using binding-based assays. We characterized the dose-response curves for five fungal pheromone G-protein-coupled receptors, peptides, and proteases -Saccharomyces cerevisiae ,  Candida albicans ,  Schizosaccharomyces pombe ,  Schizosaccharomyces octosporus , and  Schizosaccharomyces japonicus . Alanine scanning was carried out for the most selective of these- S. cerevisiae  and  C. albicans -with and without the protease. Two peptide variants were discovered, which showed diminished cleavage by the protease (CaPep2A and CaPep2A13A). Those peptides were then distinguished by utilizing the biosensor strains with and without the protease, which selectively cleaved and altered the apparent concentration of peptide required for half-maximal activation for 2 peptides-CaPep and CaPep13A, respectively-by more than one order of magnitude. These results support the hypothesis that the living yeast biosensor with a sequence-specific protease can translate single-amino-acid changes into more than one order of magnitude apparent shift in the concentration of peptide required for half-maximal activation. With further engineering by computational modeling and directed evolution, the biosensor could likely distinguish a wide variety of peptide sequences beyond the alanine scanning carried out here. In the future, we envision incorporating proteases into our living yeast biosensor for use as a point of care diagnostic, a scalable communication language, and other applications.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Crnković T, Bokor BJ, Lockwood ME, Cornish VW","authors_abbrev":"Crnković T et al.","canto_added_date":"2023-10-19 00:40:03","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Biodes Res 2023;5:0003","cv_annotations":{},"doi":"10.34133/bdr.0003","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-10-18","pubmed_publication_date":"2023","terms_by_termid":{},"title":"Peptide Variant Detection by a Living Yeast Biosensor via an Epitope-Selective Protease.","uniquename":"PMID:37849458"}


id: GO_REF:0000061
data:
  {"abstract":"We have created a standard template for classes describing molecular function involved in other biological processes. The underlying equivalence axiom template is \"P and 'part_of' some W\", where P is a molecular function and W is a biological processes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of a molecular function involved in a biological process in the Gene Ontology","uniquename":"GO_REF:0000061"}


id: PMID:10379403
data:
  {"abstract":"The order Schizosaccharomycetales contains a dimorphic and two yeast species. Sch. japonicus can form both yeast cells and mycelium, depending on the substrate and the culturing conditions. Sch. pombe is a strictly unicellular organism, but it can be forced to form mycelial cell chains by inactivating members of the sep gene family. The mutations in most of the sep genes confer pleitropic phenotypes indicating functional involvement in MAP-kinase-mediated signalling pathways. Two of them were found to encode transcription factor homologues of other eukaryotes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Sipiczki M, Grallert A, Miklós I, Zilahi E, Bozsik A, Szilágyi Z","authors_abbrev":"Sipiczki M et al.","canto_added_date":"2023-05-04 00:40:04","canto_annotation_status":"SESSION_CREATED","canto_curator_role":"JaponicusDB","canto_session_key":"eb5db4e2ead0caf4","canto_triage_status":"Cell composition or WT feature","citation":"Acta Microbiol Immunol Hung 1999;46(2-3):297-302","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1999","pubmed_entrez_date":"1999-06-24","pubmed_publication_date":"1999","terms_by_termid":{},"title":"Genetics, physiology and cytology of yeast-mycelial dimorphism in fission yeasts.","uniquename":"PMID:10379403"}


id: PMID:9720056
data:
  {"abstract":"The cells of Schizosaccharomyces japonicus var. versatilis responded to the presence of cytochalasin D (CD), an inhibitor of actin polymerization, by the disappearance of contractile actin rings (ARs) that had already formed and by inhibition of new ring formation. Actin cables disappeared. Actin patches remained preserved and became co-localized with regions of actual cell wall formation (at cell poles and at the site of septum development). Removal of the AR arrested formation of the primary septum and led to the production of aberrant septum protrusions in that region. Nuclear division was accomplished in the presence of CD but new ARs were not produced. The wall (septum) material was deposited in the form of a wide band at the inner surface of the lateral cell wall in the cell centre. This layer showed a thin fibrillar structure. The removal of CD resulted in rapid formation of new ARs in the equatorial region of the cells. This implies that the signal for AR localization was not abolished either by CD effects or by removal of an AR already formed. Some of the newly developed ARs showed atypical localization and orientation. In addition, redundant, subcortically situated actin bundles were produced. The removal of CD was quickly followed by the development of primary septa co-localized with ARs. Wall protrusions occurred co-localized with the redundant actin bundles. If these were completed in a circle, redundant septa developed. The AR is a mechanism which, in time and space, triggers cytokinesis by building a septum sequentially dependent on the AR. Aberrant septa were not capable of separating daughter cells. However, non-separated daughter cells subsequently gave rise to normal cells.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Gabriel M, Horký D, Svoboda A, Kopecká M","authors_abbrev":"Gabriel M et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Microbiology (Reading) 1998 Aug;144 ( Pt 8):2331-2344","cv_annotations":{},"doi":"10.1099/00221287-144-8-2331","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1998","pubmed_entrez_date":"1998-08-28","pubmed_publication_date":"Aug 1998","terms_by_termid":{},"title":"Cytochalasin D interferes with contractile actin ring and septum formation in Schizosaccharomyces japonicus var. versatilis.","uniquename":"PMID:9720056"}


id: PMID:23873862
data:
  {"abstract":"Many fungi respond to light and regulate fungal development and behavior. A blue light-activated complex has been identified in Neurospora crassa as the product of the wc-1 and wc-2 genes. Orthologs of WC-1 and WC-2 have hitherto been found only in filamentous fungi and not in yeast, with the exception of the basidiomycete pathogenic yeast Cryptococcus. Here, we report that the fission yeast Schizosaccharomyces japonicus responds to blue light depending on Wcs1 and Wcs2, orthologs of components of the WC complex. Surprisingly, those of ascomycete S. japonicus are more closely related to those of the basidiomycete. S. japonicus reversibly changes from yeast to hyphae in response to environmental stresses. After incubation at 30°C, a colony of yeast was formed, and then hyphal cells extended from the periphery of the colony. When light cycles were applied, distinct dark- and bright-colored hyphal cell stripes were formed because the growing hyphal cells had synchronously activated cytokinesis. In addition, temperature cycles of 30°C for 12 h and 35°C for 12 h or of 25°C for 12 h and 30°C for 12 h during incubation in the dark induced a response in the hyphal cells similar to that of light. The stripe formation of the temperature cycles was independent of the wcs genes. Both light and temperature, which are daily external cues, have the same effect on growing hyphal cells. A dual sensing mechanism of external cues allows organisms to adapt to daily changes of environmental alteration. ","alleles_by_uniquename":{"SJAG_02860:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02860","name":"wcs1delta","uniquename":"SJAG_02860:allele-1"},"SJAG_05242:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_05242","name":"wcs2delta","uniquename":"SJAG_05242:allele-1"}},"annotation_curators":[{"annotation_count":7,"community_curator":true,"file_name":null,"file_type":null,"name":"Sho Okamoto","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-12-01","authors":"Okamoto S, Furuya K, Nozaki S, Aoki K, Niki H","authors_abbrev":"Okamoto S et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2022-12-01 10:29:08","canto_curator_name":"Sho Okamoto","canto_curator_role":"community","canto_first_approved_date":"2022-12-01 10:29:08","canto_session_key":"0e71b7054e7d7754","canto_session_submitted_date":"2022-12-01 10:28:58","canto_triage_status":"Curatable","citation":"Eukaryot Cell 2013 Sep;12(9):1235-43","cv_annotations":{"biological_process":[{"annotations":[115140,115141],"is_not":false,"summary":null,"term":"GO:0071483"}],"molecular_function":[{"annotations":[115139],"is_not":false,"summary":null,"term":"GO:0009882"}],"single_locus_phenotype":[{"annotations":[115142,115143],"is_not":false,"summary":null,"term":"FYPO:0008031"},{"annotations":[115144,115145],"is_not":false,"summary":null,"term":"FYPO:0008046"}]},"doi":"10.1128/EC.00109-13","gene_count":2,"genes_by_uniquename":{"SJAG_02860":null,"SJAG_05242":null},"genotypes_by_uniquename":{"wcs1delta":{"display_name":"wcs1delta","display_uniquename":"wcs1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02860:allele-1","expression":"Null"}]}]},"wcs2delta":{"display_name":"wcs2delta","display_uniquename":"wcs2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_05242:allele-1","expression":"Null"}]}]}},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2013","pubmed_entrez_date":"2013-07-23","pubmed_publication_date":"Sep 2013","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000126":null,"FYPO:0008031":null,"FYPO:0008046":null,"FYPO_EXT:0000001":null,"GO:0009882":null,"GO:0071483":null},"title":"Synchronous activation of cell division by light or temperature stimuli in the dimorphic yeast Schizosaccharomyces japonicus.","uniquename":"PMID:23873862"}


id: PMID:28228545
data:
  {"abstract":"Inactivation of retrotransposons is accompanied by the emergence of centromere-binding protein-B (CENPB) in  Schizosaccharomyces , as well as in metazoans. The RNA interference (RNAi)-induced transcriptional silencing (RITS) complex, comprising chromodomain protein-1 (Chp1), Tas3 (protein with unknown function), and Argonaute (Ago1), plays an important role in RNAi-mediated heterochromatinization. We find that whereas the Ago1 subunit of the RITS complex is highly conserved, Tas3 is lost and Chp1 is truncated in  Schizosaccharomyces cryophilus  and  Schizosaccharomyces octosporus  We show that truncated Chp1 loses the property of heterochromatin localization and silencing when transformed in  Schizosaccharomyces pombe  Furthermore, multiple copies of CENPB, related to  Tc1/mariner and Tc5  transposons, occur in all  Schizosaccharomyces  species, as well as in humans, but with loss of transposase function (except  Schizosaccharomyces japonicus ). We propose that acquisition of  Tc1/mariner and Tc5  elements by horizontal transfer in  S. pombe  (and humans) is accompanied by alteration of their function from a transposase/endonuclease to a heterochromatin protein, designed to suppress transposon expression and recombination. The resulting redundancy of RITS may have eased the selection pressure, resulting in progressive loss or truncation of  tas3  and  chp1  genes in  S. octosporus  and  S. cryophilus  and triggered similar evolutionary dynamics in the metazoan orthologues.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Upadhyay U, Srivastava S, Khatri I, Nanda JS, Subramanian S, Arora A, Singh J","authors_abbrev":"Upadhyay U et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Phylogeny and evolutionary studies","citation":"Mol Biol Cell 2017 Apr 15;28(8):1132-1146","cv_annotations":{},"doi":"10.1091/mbc.E16-07-0485","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2017-02-24","pubmed_publication_date":"15 Apr 2017","terms_by_termid":{},"title":"Ablation of RNA interference and retrotransposons accompany acquisition and evolution of transposases to heterochromatin protein CENPB.","uniquename":"PMID:28228545"}


id: PMID:25318672
data:
  {"abstract":"Excess fatty acids and sterols are stored as triacylglycerols and sterol esters in specialized cellular organelles, called lipid droplets. Understanding what determines the cellular amount of neutral lipids and their packaging into lipid droplets is of fundamental and applied interest. Using two species of fission yeast, we show that cycling cells deficient in the function of the ER-resident CDP-DG synthase Cds1 exhibit markedly increased triacylglycerol content and assemble large lipid droplets closely associated with the ER membranes. We demonstrate that these unusual structures recruit the triacylglycerol synthesis machinery and grow by expansion rather than by fusion. Our results suggest that interfering with the CDP-DG route of phosphatidic acid utilization rewires cellular metabolism to adopt a triacylglycerol-rich lifestyle reliant on the Kennedy pathway. ","alleles_by_uniquename":{"SJAG_00426:allele-1":{"allele_type":"amino_acid_mutation","description":"P363S","gene_uniquename":"SJAG_00426","name":"bbl1-P363S","uniquename":"SJAG_00426:allele-1"}},"annotation_curators":[{"annotation_count":8,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-05-17","authors":"He Y, Yam C, Pomraning K, Chin JS, Yew JY, Freitag M, Oliferenko S","authors_abbrev":"He Y et al.","canto_added_date":"2021-05-10 02:38:06","canto_annotation_status":"APPROVED","canto_approved_date":"2021-05-17 12:42:41","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-05-17 12:42:41","canto_session_key":"f89ee2d26032c510","canto_session_submitted_date":"2021-05-17 12:42:28","canto_triage_status":"Curatable","citation":"Mol Biol Cell 2014 Dec 15;25(25):4083-95","cv_annotations":{"biological_process":[{"annotations":[115565],"is_not":false,"summary":null,"term":"GO:0016024"}],"cellular_component":[{"annotations":[115566],"is_not":false,"summary":null,"term":"GO:0005783"}],"molecular_function":[{"annotations":[115564],"is_not":false,"summary":null,"term":"GO:0004605"}],"single_locus_phenotype":[{"annotations":[115568],"is_not":false,"summary":null,"term":"FYPO:0000356"},{"annotations":[115567],"is_not":false,"summary":null,"term":"FYPO:0006433"},{"annotations":[115570],"is_not":false,"summary":null,"term":"FYPO:0004695"},{"annotations":[115569],"is_not":false,"summary":null,"term":"FYPO:0002227"},{"annotations":[115571],"is_not":false,"summary":null,"term":"FYPO:0001357"}]},"doi":"10.1091/mbc.E14-03-0832","gene_count":1,"genes_by_uniquename":{"SJAG_00426":null},"genotypes_by_uniquename":{"bbl1-P363S-P363S-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"bbl1-P363S(aa)","display_uniquename":"bbl1-P363S-P363S-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00426:allele-1","expression":"Not assayed or wild type"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2014","pubmed_entrez_date":"2014-10-17","pubmed_publication_date":"15 Dec 2014","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000006":null,"FYECO:0000162":null,"FYPO:0000356":null,"FYPO:0001357":null,"FYPO:0002227":null,"FYPO:0004695":null,"FYPO:0006433":null,"FYPO_EXT:0000001":null,"GO:0004605":null,"GO:0005783":null,"GO:0008654":null,"GO:0016024":null},"title":"Increase in cellular triacylglycerol content and emergence of large ER-associated lipid droplets in the absence of CDP-DG synthase function.","uniquename":"PMID:25318672"}


id: PMID:33495454
data:
  {"abstract":"The endoplasmic reticulum (ER) network consists of tubules with high membrane curvature in cross-section, generated by the reticulons and REEPs. These proteins have two pairs of trans-membrane (TM) segments, followed by an amphipathic helix (APH), but how they induce curvature is poorly understood. Here, we show that REEPs form homodimers by interaction within the membrane. When overexpressed or reconstituted at high concentrations with phospholipids, REEPs cause extreme curvature through their TMs, generating lipoprotein particles instead of vesicles. The APH facilitates curvature generation, as its mutation prevents ER network formation of reconstituted proteoliposomes, and synthetic L- or D-amino acid peptides abolish ER network formation in Xenopus egg extracts. In Schizosaccharomyces japonicus, the APH is required for reticulon's exclusive ER-tubule localization and restricted mobility. Thus, the TMs and APH cooperate to generate high membrane curvature. We propose that the formation of splayed REEP/reticulon dimers is responsible for ER tubule formation.","alleles_by_uniquename":{"SJAG_01374:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01374","name":"nup132delta","uniquename":"SJAG_01374:allele-1"}},"annotation_curators":[{"annotation_count":8,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-09","authors":"Wang N, Clark LD, Gao Y, Kozlov MM, Shemesh T, Rapoport TA","authors_abbrev":"Wang N et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-07-09 16:24:24","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-09 16:24:24","canto_session_key":"23c6ae79d435aba5","canto_session_submitted_date":"2021-07-09 16:24:16","canto_triage_status":"Curatable","citation":"Nat Commun 2021 01 25;12(1):568","cv_annotations":{"biological_process":[{"annotations":[115443,115449],"is_not":false,"summary":null,"term":"GO:0097753"}],"cellular_component":[{"annotations":[115444,115445],"is_not":false,"summary":null,"term":"GO:0032541"},{"annotations":[115446,115447],"is_not":false,"summary":null,"term":"GO:0005643"}],"single_locus_phenotype":[{"annotations":[115448],"is_not":false,"summary":null,"term":"FYPO:0003973"}]},"doi":"10.1038/s41467-020-20625-y","gene_count":4,"genes_by_uniquename":{"SJAG_01374":null,"SJAG_01834":null,"SJAG_01848":null,"SJAG_03795":null},"genotypes_by_uniquename":{"nup132delta":{"display_name":"nup132delta","display_uniquename":"nup132delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01374:allele-1","expression":"Null"}]}]}},"ltp_gene_count":4,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_03795","interactor_uniquename":"SJAG_03795","reference_uniquename":"PMID:33495454","throughput":"low"}],"publication_year":"2021","pubmed_entrez_date":"2021-01-26","pubmed_publication_date":"25 01 2021","terms_by_termid":{"FYPO:0003973":null,"GO:0005643":null,"GO:0032541":null,"GO:0097753":null},"title":"Mechanism of membrane-curvature generation by ER-tubule shaping proteins.","uniquename":"PMID:33495454"}


id: GO_REF:0000071
data:
  {"abstract":"We have created a standard template for classes describing the response to and cellular response to a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom templates are \"GO:0050896 and 'has input' some X\" (response to) and \"GO:0070887 and 'has input' some X\" (cellular response to), where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of response to and cellular response to a chemical as biological process in the Gene Ontology","uniquename":"GO_REF:0000071"}


id: PMID:9396147
data:
  {"abstract":"Both living and fixed cells of Schizosaccharomyces japonicus var. versatilis showed thread-like mitochondria when studied by phase-contrast and fluorescence microscopy. In the interphase cells, mitochondria extended from pole to pole and converged towards the growing tips. The mitochondrial threads did not disrupt but persisted during mitosis and, subsequently, their bundle was split between the two daughter cells by a concentrically growing septum. Mitochondria in the interphase cells were accompanied by cytoplasmic microtubules. These disappeared during mitosis and, instead, spindle microtubules were formed in the nucleus. The cytoplasmic microtubules reappeared after anaphase B, again in coaligment with mitochondria. Protoplasting as well as the action of microtubule inhibitors methyl-1-(butylcarbamoyl)-2-benzimidazolecarbamate (benomyl) and 2-methylbenzimidazole (MBC) resulted in rapid disintegration of microtubules and, suprisingly, also in disruption of mitochondria into small bodies. Removal of the inhibitors or a short regeneration of protoplasts allowed both the cytoplasmic microtubules and the thread-like mitochondria to reaggregate into the original pattern. Cytochalasin D treatment caused a complete disintegration of actin filaments, while the cytoplasmic microtubules and mitochondria remained intact. These findings of a transient close association of mitochondria and microtubules and their relative independence of the arrangement of actin filaments suggest that microtubules, but not actin cables, form supports for positioning or movement of mitochondria along the cylindrical cells. The persistence of mitochondria in the cell centre during mitosis may be accounted for by the fact that disrupted microtubules fail to provide support for mitochondrial movement towards the cell poles.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Svoboda A, Slaninová I","authors_abbrev":"Svoboda A et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Can J Microbiol 1997 Oct;43(10):945-53","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1997","pubmed_entrez_date":"1997-12-13","pubmed_publication_date":"Oct 1997","terms_by_termid":{},"title":"Colocalization of microtubules and mitochondria in the yeast Schizosaccharomyces japonicus var. versatilis.","uniquename":"PMID:9396147"}


id: PMID:11504450
data:
  {"abstract":"We compared the effects of four quaternary benzo[c]phenanthridine alkaloids--chelerythrine, chelilutine, sanguinarine, and sanguilutine--and two quaternary protoberberine alkaloids-berberine and coptisine--on the human cell line HeLa (cervix carcinoma cells) and the yeasts Saccharomyces cerevisiae and Schizosaccharomyces japonicus var. versatilis. The ability of alkaloids to display primary fluorescence, allowed us to record their dynamics and localization in cells. Cytotoxic, anti-microtubular, and anti-actin effects in living cells were studied. In the yeasts, neither microtubules nor cell growth was seriously affected even at the alkaloid concentration of 100 microg/ml. The HeLa cells, however, responded to the toxic effect of alkaloids at concentrations ranging from 1 to 50 microg/ml. IC50 values for individual alkaloids were: sanguinarine IC50 = 0.8 microg/ml, sanguilutine IC50 = 8.3 microg/ml, chelerythrine IC50 = 6.2 microg/ml, chelilutine IC50 = 5.2 microg/ml, coptisine IC50 = 2.6 microg/ml and berberine IC50 > 10.0 microg/ml. In living cells, sanguinarine produced a decrease in microtubule numbers, particularly at the cell periphery, at a concentration of 0.1 microg/ml. The other alkaloids showed a similar effect but at higher concentrations (5-50 microg/ml). The strongest effects of sanguinarine were explained as a consequence of its easy penetration through the cell membrane owing to nonpolar pseudobase formation and to a high degree of molecular planarity.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Slaninová I, Táborská E, Bochoráková H, Slanina J","authors_abbrev":"Slaninová I et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Cell Biol Toxicol 2001;17(1):51-63","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2001","pubmed_entrez_date":"2001-08-16","pubmed_publication_date":"2001","terms_by_termid":{},"title":"Interaction of benzo[c]phenanthridine and protoberberine alkaloids with animal and yeast cells.","uniquename":"PMID:11504450"}


id: PMID:35940784
data:
  {"abstract":"Schizosaccharomyces japonicus have been found as dominant yeast species coexisting with Saccharomyces cerevisiae during late stages of spontaneous fermentation of local grapes in Guizhou, China. Therefore, this study further investigated the impacts of the two indigenous yeast species on typicality of crystal grape (Niagara) wine. Five indigenous and one commercial S. cerevisiae strains were firstly selected based on their genotypes and fermentation traits in synthetic medium. All the six S. cerevisiae exhibited high tolerance to glucose, temperature, and SO 2 . The two killer active strains FBKL2.996 and FBKL2.9126 showed relative higher tolerance capacity of ethanol, pH and osmotic pressure than the other four S. cerevisiae strains. Further pure fermentation of six strains using crystal grape must exhibited different contents of volatile compounds, with commercial strain CECA producing the highest levels of acetate esters (phenethyl acetate), ethyl esters (ethyl caprylate, ethyl hexanoate), n-caprylic acid isobutyl ester, and terpenes (linalool) whereas being ranked the last in the sensory analysis. The co-inoculation of indigenous S. japonicus with each of the six S. cerevisiae strains increased the acetate esters (mainly isoamyl acetate) by 2-3 times in crystal grape wine. The indigenous S. cerevisiae FBKL2.9128 showed the most obvious variation of volatile compounds between pure and mixed fermentation, exhibiting the significant increase of isoamyl acetate, ethyl decanoate, ethyl caprylate, ethyl hexanoate, methyl decanoate, and dodecanal when co-inoculated with S. japonicus. Sugar addition in immature crystal grape juice increased the ethanol, glycerol, and some volatile compounds such as ethyl butyrate, but decreased the volatile compounds with floral and animal odors. The aroma sensory analysis confirmed the decrease of varietal aroma in wines with sugar addition when comparing with wines made from immature crystal grape. The results of this study provide basic information on the impact of indigenous S. cerevisaie and S. japonicus, and sugar addition on typicality of crystal grape wine, which would help to improve the wine flavor made from crystal grape in southwest China.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Wang C, Liang S, Yang J, Wu C, Qiu S","authors_abbrev":"Wang C et al.","canto_added_date":"2023-05-04 00:40:03","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Food Res Int 2022 Sep;159:111580","cv_annotations":{},"doi":"10.1016/j.foodres.2022.111580","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-08-08","pubmed_publication_date":"Sep 2022","terms_by_termid":{},"title":"The impact of indigenous Saccharomyces cerevisiae and Schizosaccharomyces japonicus on typicality of crystal grape (Niagara) wine.","uniquename":"PMID:35940784"}


id: PMID:31380845
data:
  {"abstract":"Lipid metabolism and its regulation are of interest to both basic and applied life sciences and biotechnology. In this regard, various yeast species are used as models in lipid metabolic research or for industrial lipid production. Lipid droplets are highly dynamic storage bodies and their cellular content represents a convenient readout of the lipid metabolic state. Fluorescence microscopy is a method of choice for quantitative analysis of cellular lipid droplets, as it relies on widely available equipment and allows analysis of individual lipid droplets. Furthermore, microscopic image analysis can be automated, greatly increasing overall analysis throughput. Here, we describe an experimental and analytical workflow for automated detection and quantitative description of individual lipid droplets in three different model yeast species: the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus, and the budding yeast Saccharomyces cerevisiae. Lipid droplets are visualized with BODIPY 493/503, and cell-impermeable fluorescent dextran is added to the culture media to help identify cell boundaries. Cells are subjected to 3D epifluorescence microscopy in green and blue channels and the resulting z-stack images are processed automatically by a MATLAB pipeline. The procedure outputs rich quantitative data on cellular lipid droplet content and individual lipid droplet characteristics in a tabular format suitable for downstream analyses in major spreadsheet or statistical packages. We provide example analyses of lipid droplet content under various conditions that affect cellular lipid metabolism.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Princová J, Schätz M, Ťupa O, Převorovský M","authors_abbrev":"Princová J et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"J Vis Exp 2019 07 17;(149)","cv_annotations":{},"doi":"10.3791/59889","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2019","pubmed_entrez_date":"2019-08-06","pubmed_publication_date":"17 07 2019","terms_by_termid":{},"title":"Analysis of Lipid Droplet Content in Fission and Budding Yeasts using Automated Image Processing.","uniquename":"PMID:31380845"}


id: GO_REF:0000044
data:
  {"abstract":"Transitive assignment of GO terms based on the UniProtKB/Swiss-Prot Subcellular Location vocabulary. UniProtKB Subcellular Location is a controlled vocabulary used to supply subcellular location information to UniProtKB entries in the SUBCELLULAR LOCATION lines. Terms from this vocabulary are annotated manually to UniProtKB/Swiss-Prot entries but are automatically assigned to UniProtKB/TrEMBL entries from the underlying nucleic acid databases and/or by the UniProt automatic annotation program.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"UniProt-GOA","canto_curator_role":"JaponicusDB","cv_annotations":{"cellular_component":[{"annotations":[65983],"is_not":false,"summary":null,"term":"GO:0001725"},{"annotations":[67139],"is_not":false,"summary":null,"term":"GO:0031982"}]},"gene_count":2,"genes_by_uniquename":{"SJAG_01739":null,"SJAG_03357":null},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{"GO:0001725":null,"GO:0031982":null},"title":"Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt. ","uniquename":"GO_REF:0000044"}


id: GO_REF:0000091
data:
  {"abstract":"We have created a standard template for classes describing the cell migration process for a cell type as a biological process. The underlying equivalence axiom template is \"'cell migration' and 'alters_location_of' some C\", where C is a native cell (CL:0000004).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of cell migration as biological processes in the Gene Ontology","uniquename":"GO_REF:0000091"}


id: GO_REF:0000004
data:
  {"abstract":"Transitive assignments using UniProtKB keywords. The UniProtKB keyword controlled vocabulary has been created and used by the UniProt Knowledgebase (UniProtKB) to supply 10 different categories of information to UniProtKB entries. Further information on the UniProtKB keyword resource can be found at http://www.uniprot.org/docs/keywlist. <br>Further information on the UniProt annotation methods is available at  https://www.uniprot.org/help/manual_curation and https://www.uniprot.org/help/automatic_annotation.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GOA curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Comments","uniquename":"GO_REF:0000004"}


id: PMID:23337086
data:
  {"abstract":"During meiosis, chromosomes adopt a bouquet arrangement, which is widely conserved among eukaryotes. This arrangement is assumed to play an important role in the normal progression of meiosis, by mediating the proper pairing of homologous chromosomes. In Schizosaccharomyces pombe, the complex of Bqt1 and Bqt2 plays a key role in telomere clustering and the subsequent bouquet arrangement of chromosomes during early meiotic prophase. Bqt1 and Bqt2 are part of a multi-protein complex that mediates the attachment of the telomere to the nuclear membrane. However, the structural details of the complex are needed to clarify the mechanism of telomere clustering. To enable biophysical studies of Bqt1 and Bqt2, we established a purification procedure for the Schizosaccharomyces japonicus Bqt1-Bqt2 complex, which is closely related to the S. pombe Bqt1-Bqt2 complex. A co-expression vector, in which one of the expressed subunits is fused to a removable SUMO tag, yielded high amounts of the proteins in the soluble fraction. The solubility of the Bqt1-Bqt2 complex after the removal of the SUMO tag was maintained by including CHAPS, a nondenaturing, zwitterionic detergent, in the purification buffers. These procedures enabled us to rapidly purify the stable Bqt1-Bqt2 complex. The co-purified Bqt1 and Bqt2 proteins formed a stable heterodimer, consistent with results from in vivo studies showing the requirement of both proteins for the bouquet arrangement. The expression and purification procedures established here will facilitate further biophysical studies of the Bqt1-Bqt2 complex.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":2,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-05-12","authors":"Ichikawa Y, Kagawa W, Saito K, Chikashige Y, Haraguchi T, Hiraoka Y, Kurumizaka H","authors_abbrev":"Ichikawa Y et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-05-12 14:11:00","canto_curator_name":"Val Wood","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-05-12 14:11:00","canto_session_key":"34571f3accd180c4","canto_session_submitted_date":"2021-05-11 18:50:05","canto_triage_status":"Curatable","citation":"Protein Expr Purif 2013 Apr;88(2):207-13","cv_annotations":{"molecular_function":[{"annotations":[115392,115393],"is_not":false,"summary":null,"term":"GO:0005515"}]},"doi":"10.1016/j.pep.2013.01.006","gene_count":2,"genes_by_uniquename":{"SJAG_03287":null,"SJAG_05260":null},"genotypes_by_uniquename":{},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[{"evidence":"Co-purification","gene_uniquename":"SJAG_03287","interactor_uniquename":"SJAG_05260","reference_uniquename":"PMID:23337086","throughput":"low"}],"publication_year":"2013","pubmed_entrez_date":"2013-01-23","pubmed_publication_date":"Apr 2013","terms_by_termid":{"GO:0005515":null},"title":"Purification and characterization of the fission yeast telomere clustering factors, Bqt1 and Bqt2.","uniquename":"PMID:23337086"}


id: PMID:23150598
data:
  {"abstract":"A key question in developmental biology addresses the mechanism of asymmetric cell division. Asymmetry is crucial for generating cellular diversity required for development in multicellular organisms. As one of the potential mechanisms, chromosomally borne epigenetic difference between sister cells that changes mating/cell type has been demonstrated only in the Schizosaccharomyces pombe fission yeast. For technical reasons, it is nearly impossible to determine the existence of such a mechanism operating during embryonic development of multicellular organisms. Our work addresses whether such an epigenetic mechanism causes asymmetric cell division in the recently sequenced fission yeast, S. japonicus (with 36% GC content), which is highly diverged from the well-studied S. pombe species (with 44% GC content). We find that the genomic location and DNA sequences of the mating-type loci of S. japonicus differ vastly from those of the S. pombe species. Remarkably however, similar to S. pombe, the S. japonicus cells switch cell/mating type after undergoing two consecutive cycles of asymmetric cell divisions: only one among four \"granddaughter\" cells switches. The DNA-strand-specific epigenetic imprint at the mating-type locus1 initiates the recombination event, which is required for cellular differentiation. Therefore the S. pombe and S. japonicus mating systems provide the first two examples in which the intrinsic chirality of double helical structure of DNA forms the primary determinant of asymmetric cell division. Our results show that this unique strand-specific imprinting/segregation epigenetic mechanism for asymmetric cell division is evolutionary conserved. Motivated by these findings, we speculate that DNA-strand-specific epigenetic mechanisms might have evolved to dictate asymmetric cell division in diploid, higher eukaryotes as well.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Yu C, Bonaduce MJ, Klar AJ","authors_abbrev":"Yu C et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Genetics 2013 Jan;193(1):85-94","cv_annotations":{},"doi":"10.1534/genetics.112.146233","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2013","pubmed_entrez_date":"2012-11-15","pubmed_publication_date":"Jan 2013","terms_by_termid":{},"title":"Defining the epigenetic mechanism of asymmetric cell division of Schizosaccharomyces japonicus yeast.","uniquename":"PMID:23150598"}


id: PMID:33791858
data:
  {"abstract":"Mitogen-activated protein kinase (MAPK) signalling pathways regulate multiple cellular functions in eukaryotic organisms in response to environmental cues, including the dynamic remodeling of the actin cytoskeleton. The fission yeast S. pombe is an optimal model to investigate the conserved regulatory mechanisms of cytokinesis, which relies in an actomyosin-based contractile ring (CAR) that prompts the physical separation of daughter cells during cellular division. Our group has recently shown that p38 MAPK ortholog Sty1, the core component of the stress-activated pathway (SAPK), negatively modulates CAR assembly and integrity in S. pombe during actin cytoskeletal damage induced with Latrunculin A and in response to environmental stress. This response involves downregulation of protein levels of the formin For3, which assembles actin filaments for cables and the CAR, likely through an ubiquitin-mediated degradation mechanism. Contrariwise, Sty1 function positively reinforces CAR assembly during stress in the close relative dimorphic fission yeast S. japonicus. The opposite effect of SAPK signaling on CAR integrity may represent an evolutionary refined adaptation to cope with the marked differences in cytokinesis onset in both fission yeast species.","alleles_by_uniquename":{"SJAG_00266:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00266","name":"atf1delta","uniquename":"SJAG_00266:allele-1"},"SJAG_02592:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02592","name":"sty1delta","uniquename":"SJAG_02592:allele-1"}},"annotation_curators":[{"annotation_count":4,"community_curator":true,"file_name":null,"file_type":null,"name":"Elisa Gómez Gil","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-09-14","authors":"Madrid M, Gómez-Gil E, Cansado J","authors_abbrev":"Madrid M et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-14 21:24:28","canto_curator_name":"Elisa Gómez Gil","canto_curator_role":"community","canto_first_approved_date":"2021-09-14 21:24:28","canto_session_key":"84ac20b0ff20a3cd","canto_session_submitted_date":"2021-09-14 16:45:32","canto_triage_status":"Curatable","citation":"Curr Genet 2021 Oct;67(5):715-721","cv_annotations":{"PSI-MOD":[{"annotations":[115229],"is_not":false,"summary":null,"term":"MOD:00696"}],"single_locus_phenotype":[{"annotations":[115228],"is_not":false,"summary":null,"term":"FYPO:0002998"},{"annotations":[115226,115227],"is_not":false,"summary":null,"term":"FYPO:0000107"}]},"doi":"10.1007/s00294-021-01155-6","gene_count":2,"genes_by_uniquename":{"SJAG_00266":null,"SJAG_02592":null},"genotypes_by_uniquename":{"atf1delta":{"display_name":"atf1delta","display_uniquename":"atf1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00266:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]}},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-04-01","pubmed_publication_date":"Oct 2021","terms_by_termid":{"FYECO:0000248":null,"FYPO:0000107":null,"FYPO:0002998":null,"FYPO_EXT:0000001":null,"GO:0120306":null,"MOD:00696":null},"title":"Negative control of cytokinesis by stress-activated MAPK signaling.","uniquename":"PMID:33791858"}


id: PMID:24184107
data:
  {"abstract":"During cellular proliferation, the mother nucleus divides into two daughters, each carrying a full complement of chromosomes and capable of driving the next cell cycle. Mitotic chromosome segregation must be coordinated with remodeling of other nuclear components, including the nuclear envelope (NE) and the non-membrane-bound nucleolus. Here, we show that in the fission yeast Schizosaccharomyces japonicus, which breaks and reforms the NE during mitosis, the evolutionary conserved LEM-domain protein Man1 promotes equal partitioning of the nuclear membrane, nucleolar remodeling, and efficient inheritance of the nuclear pore complexes (NPCs) by the daughter nuclei. Analyses of man1 mutants and results obtained using an artificial chromatin-nuclear pore tether suggest that Man1 may exert its function by linking the NPCs to segregating chromatin. By integrating the partitioning of the nuclear membrane and nucleolar material with chromosome segregation, cells build two nearly identical copies of the original nucleus.","alleles_by_uniquename":{"SJAG_01834:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01834","name":"pom152delta","uniquename":"SJAG_01834:allele-1"},"SJAG_03449:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03449","name":"man1delta","uniquename":"SJAG_03449:allele-1"},"SJAG_03449:allele-2":{"allele_type":"partial_amino_acid_deletion","description":"man1DHEH","gene_uniquename":"SJAG_03449","name":"Man1DHEH","uniquename":"SJAG_03449:allele-2"},"SJAG_03449:allele-3":{"allele_type":"amino_acid_insertion_and_deletion","description":"man1-1-488","gene_uniquename":"SJAG_03449","name":"man1-1-488","uniquename":"SJAG_03449:allele-3"}},"annotation_curators":[{"annotation_count":17,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"},{"annotation_count":2,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-27","authors":"Yam C, Gu Y, Oliferenko S","authors_abbrev":"Yam C et al.","canto_added_date":"2021-05-10 02:38:18","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-01 07:25:17","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-27 11:54:17","canto_session_key":"0f2dda384385121f","canto_session_submitted_date":"2021-07-27 11:54:10","canto_triage_status":"Curatable","citation":"Curr Biol 2013 Nov 18;23(22):2303-2310","cv_annotations":{"biological_process":[{"annotations":[115220],"is_not":false,"summary":null,"term":"GO:0101024"}],"cellular_component":[{"annotations":[115205],"is_not":false,"summary":null,"term":"GO:0000781"},{"annotations":[115204],"is_not":false,"summary":null,"term":"GO:0140573"},{"annotations":[115207],"is_not":false,"summary":null,"term":"GO:0005643"},{"annotations":[115206],"is_not":false,"summary":null,"term":"GO:0030875"}],"molecular_function":[{"annotations":[115221],"is_not":false,"summary":null,"term":"GO:0062239"}],"single_locus_phenotype":[{"annotations":[115208,115213,115215],"is_not":false,"summary":null,"term":"FYPO:0003779"},{"annotations":[115217,115218,115219],"is_not":false,"summary":null,"term":"FYPO:0000671"},{"annotations":[115210,115211,115212,115214],"is_not":false,"summary":null,"term":"FYPO:0004890"},{"annotations":[115209],"is_not":false,"summary":null,"term":"FYPO:0001234"},{"annotations":[115216],"is_not":false,"summary":null,"term":"FYPO:0004683"}]},"doi":"10.1016/j.cub.2013.09.057","gene_count":5,"genes_by_uniquename":{"SJAG_00302":null,"SJAG_01777":null,"SJAG_01834":null,"SJAG_03449":null,"SJAG_03603":null},"genotypes_by_uniquename":{"Man1DHEH-man1DHEH-partial_amino_acid_deletion-expression-not_assayed_or_wild_type":{"display_name":"Man1DHEH(man1DHEH)","display_uniquename":"Man1DHEH-man1DHEH-partial_amino_acid_deletion-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03449:allele-2","expression":"Not assayed or wild type"}]}]},"man1-1-488-man1-1-488-amino_acid_insertion_and_deletion-expression-not_assayed_or_wild_type":{"display_name":"man1-1-488(aa)","display_uniquename":"man1-1-488-man1-1-488-amino_acid_insertion_and_deletion-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03449:allele-3","expression":"Not assayed or wild type"}]}]},"man1delta":{"display_name":"man1delta","display_uniquename":"man1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03449:allele-1","expression":"Null"}]}]},"pom152delta":{"display_name":"pom152delta","display_uniquename":"pom152delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01834:allele-1","expression":"Null"}]}]}},"ltp_gene_count":5,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2013","pubmed_entrez_date":"2013-11-05","pubmed_publication_date":"18 Nov 2013","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000162":null,"FYPO:0000671":null,"FYPO:0001234":null,"FYPO:0003779":null,"FYPO:0004683":null,"FYPO:0004890":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null,"GO:0000781":null,"GO:0005643":null,"GO:0030875":null,"GO:0062239":null,"GO:0101024":null,"GO:0140573":null},"title":"Partitioning and remodeling of the Schizosaccharomyces japonicus mitotic nucleus require chromosome tethers.","uniquename":"PMID:24184107"}


id: GO_REF:0000060
data:
  {"abstract":"We have created a standard template for classes describing processes involved in other processes. The underlying equivalence axiom template is \"P and 'part_of' some W\", where P and W are biological processes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of processes involved in other process in the Gene Ontology","uniquename":"GO_REF:0000060"}


id: GO_REF:0000062
data:
  {"abstract":"We have created a standard template for classes describing processes occurring in parts of the cell. The underlying equivalence axiom template is \"P and 'occurs in' some C\", where P is a biological process and C is a cellular component.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of processes occurring in parts of the cell in the Gene Ontology","uniquename":"GO_REF:0000062"}


id: GO_REF:0000116
data:
  {"abstract":"Rhea (https://www.rhea-db.org/, PMID:30272209) is an expert-curated knowledgebase of chemical and transport reactions of biological interest - and the standard for enzyme and transporter annotation in UniProtKB (PMID:31688925). Rhea uses the chemical dictionary ChEBI (Chemical Entities of Biological Interest) to describe reaction participants and their chemical transformations in a computationally tractable manner. GO terms corresponding to Rhea reactions are assigned a Rhea database cross-reference. The corresponding GO term is automatically applied to all UniProt entries annotated with a Rhea reaction. The mapping file is available at: http://current.geneontology.org/ontology/external2go/rhea2go.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO Central curators, GOA curators, Rhea curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Automatic Gene Ontology annotation based on Rhea mapping.","uniquename":"GO_REF:0000116"}


id: PMID:35359202
data:
  {"abstract":"The fission yeast genus Schizosaccharomyces contains important model organisms for biological research. In particular, S. pombe is a widely used model eukaryote. So far little is known about the natural and artificial habitats of species in this genus. Finding out where S. pombe and other fission yeast species occur and how they live in their habitats can promote better understanding of their biology. Here we investigate in which substrates S. pombe, S. octosporus, S. osmophilus and S. japonicus are present. To this end about 2100 samples consisting of soil, tree sap fluxes, fresh fruit, dried fruit, honey, cacao beans, molasses and other substrates were analyzed. Effective isolation methods that allow efficient isolation of the above mentioned species were developed. Based on the frequency of isolating different fission yeast species in various substrates and on extensive literature survey, conclusions are drawn on their ecology. The results suggest that the primary habitat of S. pombe and S. octosporus is honeybee honey. Both species were also frequently detected on certain dried fruit like raisins, mango or pineapple to which they could be brought by the honey bees during ripening or during drying. While S. pombe was regularly isolated from grape mash and from fermented raw cacao beans S. octosporus was never isolated from fresh fruit. The main habitat of S. osmophilus seems to be solitary bee beebread. It was rarely isolated from raisins. S. japonicus was mainly found in forest substrates although it occurs on fruit and in fruit fermentations, too.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Brysch-Herzberg M, Jia GS, Seidel M, Assali I, Du LL","authors_abbrev":"Brysch-Herzberg M et al.","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Phylogeny and evolutionary studies","citation":"Antonie Van Leeuwenhoek 2022 May;115(5):661-695","cv_annotations":{},"doi":"10.1007/s10482-022-01720-0","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-04-01","pubmed_publication_date":"May 2022","terms_by_termid":{},"title":"Insights into the ecology of Schizosaccharomyces species in natural and artificial habitats.","uniquename":"PMID:35359202"}


id: PMID:7214237
data:
  {"abstract":"Hybridization studies based on the prototrophic selection technique, involving the use of auxotrophic mutants of strains of five accepted species of the genus Schizosaccharomyces, are reported. Intrastrain recombinants were recovered in five out of six tested parental pairs. Interstrain recombinants were recovered from crosses involving strains of S. japonicus and strains of S. pombe. No recombinants were recovered in 62 interspecific crosses involving all possible combinations of the six representatives of the genus.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Johannsen E","authors_abbrev":"Johannsen E","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Can J Microbiol 1981 Feb;27(2):184-91","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1981","pubmed_entrez_date":"1981-02-01","pubmed_publication_date":"Feb 1981","terms_by_termid":{},"title":"Hybridization studies within the genus Schizosaccharomyces Lindner.","uniquename":"PMID:7214237"}


id: GO_REF:0000088
data:
  {"abstract":"We have created a standard template for classes defining a protein complex by a molecular function as a cellular component. The underlying equivalence axiom template is \"GO:0043234 and 'capable_of' some ?A\", where A is a molecular function.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of protein complex by molecular function in the Gene Ontology","uniquename":"GO_REF:0000088"}


id: GO_REF:0000081
data:
  {"abstract":"We have created a standard template for classes describing the formation of a plant structure as a biological process. The underlying equivalence axiom template is \"'anatomical structure formation involved in morphogenesis' and 'results in formation of' some P\", where P is a plant anatomical entity (PO:0025131).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of plant formation as biological process in the Gene Ontology","uniquename":"GO_REF:0000081"}


id: PMID:35380656
data:
  {"abstract":"The fission yeast Schizosaccharomyces japonicus has recently emerged as a powerful system for studying the evolution of essential cellular processes, drawing on similarities as well as key differences between S. japonicus and the related, well-established model Schizosaccharomyces pombe. We have deployed the open-source, modular code and tools originally developed for PomBase, the S. pombe model organism database (MOD), to create JaponicusDB (www.japonicusdb.org), a new MOD dedicated to S. japonicus. By providing a central resource with ready access to a growing body of experimental data, ontology-based curation, seamless browsing and querying, and the ability to integrate new data with existing knowledge, JaponicusDB supports fission yeast biologists to a far greater extent than any other source of S. japonicus data. JaponicusDB thus enables S. japonicus researchers to realize the full potential of studying a newly emerging model species and illustrates the widely applicable power and utility of harnessing reusable PomBase code to build a comprehensive, community-maintainable repository of species-relevant knowledge.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Rutherford KM, Harris MA, Oliferenko S, Wood V","authors_abbrev":"Rutherford KM et al.","canto_added_date":"2023-05-04 00:40:03","canto_curator_role":"JaponicusDB","canto_triage_status":"Database","citation":"Genetics 2022 Apr 04;220(4)","cv_annotations":{},"doi":"10.1093/genetics/iyab223","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-04-05","pubmed_publication_date":"04 Apr 2022","terms_by_termid":{},"title":"JaponicusDB: rapid deployment of a model organism database for an emerging model species.","uniquename":"PMID:35380656"}


id: PMID:32915139
data:
  {"abstract":"Cytokinesis, which enables the physical separation of daughter cells once mitosis has been completed, is executed in fungal and animal cells by a contractile actin- and myosin-based ring (CAR). In the fission yeast  Schizosaccharomyces pombe,  the formin For3 nucleates actin cables and also co-operates for CAR assembly during cytokinesis. Mitogen-activated protein kinases (MAPKs) regulate essential adaptive responses in eukaryotic organisms to environmental changes. We show that the stress-activated protein kinase pathway (SAPK) and its effector, MAPK Sty1, downregulates CAR assembly in  S. pombe  when its integrity becomes compromised during cytoskeletal damage and stress by reducing For3 levels. Accurate control of For3 levels by the SAPK pathway may thus represent a novel regulatory mechanism of cytokinesis outcome in response to environmental cues. Conversely, SAPK signaling favors CAR assembly and integrity in its close relative  Schizosaccharomyces japonicus,  revealing a remarkable evolutionary divergence of this response within the fission yeast clade.","alleles_by_uniquename":{"SJAG_00266:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00266","name":"atf1delta","uniquename":"SJAG_00266:allele-1"},"SJAG_02592:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02592","name":"sty1delta","uniquename":"SJAG_02592:allele-1"}},"annotation_curators":[{"annotation_count":5,"community_curator":true,"file_name":null,"file_type":null,"name":"Elisa Gómez Gil","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-05-13","authors":"Gómez-Gil E, Martín-García R, Vicente-Soler J, Franco A, Vázquez-Marín B, Prieto-Ruiz F, Soto T, Pérez P, Madrid M, Cansado J","authors_abbrev":"Gómez-Gil E et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2023-06-24 05:18:12","canto_curator_name":"Elisa Gómez Gil","canto_curator_role":"community","canto_first_approved_date":"2021-05-13 16:19:42","canto_session_key":"382ba25ae62a1134","canto_session_submitted_date":"2021-05-13 14:28:51","canto_triage_status":"Curatable","citation":"Elife 2020 09 11;9","cv_annotations":{"PSI-MOD":[{"annotations":[115202],"is_not":false,"summary":null,"term":"MOD:00696"}],"biological_process":[{"annotations":[115203],"is_not":false,"summary":null,"term":"GO:1903499"}],"single_locus_phenotype":[{"annotations":[115201],"is_not":false,"summary":null,"term":"FYPO:0002998"},{"annotations":[115199,115200],"is_not":false,"summary":null,"term":"FYPO:0000107"}]},"doi":"10.7554/eLife.57951","gene_count":2,"genes_by_uniquename":{"SJAG_00266":null,"SJAG_02592":null},"genotypes_by_uniquename":{"atf1delta":{"display_name":"atf1delta","display_uniquename":"atf1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00266:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]}},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2020","pubmed_entrez_date":"2020-09-11","pubmed_publication_date":"11 09 2020","terms_by_termid":{"FYECO:0000137":null,"FYECO:0000248":null,"FYPO:0000107":null,"FYPO:0002998":null,"FYPO_EXT:0000001":null,"GO:0120306":null,"GO:1903499":null,"MOD:00696":null},"title":"Stress-activated MAPK signaling controls fission yeast actomyosin ring integrity by modulating formin For3 levels.","uniquename":"PMID:32915139"}


id: GO_REF:0000054
data:
  {"abstract":"LIFEdb is a database that was created to manage the experimental data produced by the German Cancer Research Institute (DKFZ) and its collaborators, from work on cDNAs contained in the German cDNA Consortium collection. <br>A novel cloning technology was used to rapidly generate N- and C-terminal green fluorescent protein fusions of cDNAs to examine the intracellular localizations of expressed fusion proteins in living cells. GO Cellular Component terms are manually assigned by curators studying fluorescence microscope images of cells labelled with GFP-fused cDNAs. Protein coding regions of novel full length cDNAs are tagged with the coding sequence of the green fluorescent protein, the fusion proteins are then expressed and analyzed for their subcellular localization. <br>Prior to February 2013, all LIFEdb annotations were referenced by PMID: 11256614 (Simpson et al. 2000 EMBO Rep. 1:287-292), a paper describing the protein subcellular localization pilot study and methodology used by LIFEdb. However, it has been decided that these annotations are more correctly described by a GO reference. <br>Resource URL: http://www.dkfz.de/en/mga/Groups/LIFEdb-Database.html <br>Protein subcellular localization images can be viewed on the LIFEdb website, http://www.dkfz.de/gpcf/lifedb.php","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"LIFEdb","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells.","uniquename":"GO_REF:0000054"}


id: GO_REF:0000074
data:
  {"abstract":"We have created a standard template for classes describing the export of a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom template is \"GO:0006810 and 'exports' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of export of a chemical as biological process in the Gene Ontology","uniquename":"GO_REF:0000074"}


id: GO_REF:0000003
data:
  {"abstract":"Transitive assignment using Enzyme Commission identifiers. This method is used for any database entry, such as a protein record in UniProtKB or TrEMBL, that has had an Enzyme Commission number assigned. The corresponding GO term is determined using the EC cross-references in the GO molecular function ontology. Also see Hill et al., Genomics (2001) 74:121-128. The mapping file is available at http://www.geneontology.org/external2go/ec2go.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GOA curators, MGI curators","canto_curator_role":"JaponicusDB","cv_annotations":{"molecular_function":[{"annotations":[67302],"is_not":false,"summary":null,"term":"GO:0003870"},{"annotations":[64896],"is_not":false,"summary":null,"term":"GO:0003986"},{"annotations":[69168],"is_not":false,"summary":null,"term":"GO:0003925"},{"annotations":[59186],"is_not":false,"summary":null,"term":"GO:0043864"},{"annotations":[65735],"is_not":false,"summary":null,"term":"GO:0052832"},{"annotations":[65736],"is_not":false,"summary":null,"term":"GO:0052833"},{"annotations":[68782],"is_not":false,"summary":null,"term":"GO:1990817"},{"annotations":[61249],"is_not":false,"summary":null,"term":"GO:0102389"},{"annotations":[60060],"is_not":false,"summary":null,"term":"GO:0003983"}]},"gene_count":8,"genes_by_uniquename":{"SJAG_00097":null,"SJAG_02178":null,"SJAG_02383":null,"SJAG_02721":null,"SJAG_02985":null,"SJAG_03739":null,"SJAG_04509":null,"SJAG_04954":null},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{"GO:0003870":null,"GO:0003925":null,"GO:0003983":null,"GO:0003986":null,"GO:0043864":null,"GO:0052832":null,"GO:0052833":null,"GO:0102389":null,"GO:1990817":null},"title":"Gene Ontology annotation based on Enzyme Commission mapping","uniquename":"GO_REF:0000003"}


id: PMID:29566183
data:
  {"abstract":"Dimorphic yeasts transform into filamentous cells or hyphae in response to environmental cues. The mechanisms for the hyphal transition of dimorphic yeasts have mainly been studied in Candida albicans, an opportunistic human fungal pathogen. The Ras1-MAPK pathway is a major signal transduction pathway for hyphal transition in C. albicans. Recently, the non-pathogenic dimorphic yeast Schizosaccharomyces japonicus has also been used for genetic analyses of hyphal induction. We confirmed that Ras1-MAPK and other MAPK pathways exist in Sz. japonicus. To examine how hyphal transition is induced by environmental stress-triggered signal transduction, we studied the hyphal transition of deletion mutants of MAPK pathways in Sz. japonicus. We found that the MAPK pathways are not involved in hyphal induction, although the mating response is dependent on these pathways. However, only Ras1 deletion caused a severe defect in hyphal development via both DNA damage and environmental stressors. In fact, genes on the Cdc42 branch of the Ras1 (Ras1-Cdc42) pathway, efc25Sj, scd1Sj and scd2Sj, are required for hyphal development. Cell morphology analysis indicated that the apical growth of hyphal cells was inhibited in Ras1-Cdc42-pathway deletion mutants. Thus, the control of cell polarity by the Ras1-Cdc42 pathway is crucial for hyphal development.","alleles_by_uniquename":{"SJAG_00514:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00514","name":"scd1delta","uniquename":"SJAG_00514:allele-1"},"SJAG_00993:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00993","name":"byr1delta","uniquename":"SJAG_00993:allele-1"},"SJAG_01181:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01181","name":"pek1delta","uniquename":"SJAG_01181:allele-1"},"SJAG_01718:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01718","name":"byr2delta","uniquename":"SJAG_01718:allele-1"},"SJAG_01794:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01794","name":"scd2delta","uniquename":"SJAG_01794:allele-1"},"SJAG_02342:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02342","name":"wis1delta","uniquename":"SJAG_02342:allele-1"},"SJAG_02379:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02379","name":"gap1delta","uniquename":"SJAG_02379:allele-1"},"SJAG_02486:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02486","name":"ste6delta","uniquename":"SJAG_02486:allele-1"},"SJAG_02592:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02592","name":"sty1delta","uniquename":"SJAG_02592:allele-1"},"SJAG_02819:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02819","name":"efc25delta","uniquename":"SJAG_02819:allele-1"},"SJAG_02923:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02923","name":"spk1delta","uniquename":"SJAG_02923:allele-1"},"SJAG_03384:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03384","name":"wis4delta","uniquename":"SJAG_03384:allele-1"},"SJAG_03453:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03453","name":"ras1delta","uniquename":"SJAG_03453:allele-1"},"SJAG_03753:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03753","name":"mkh1delta","uniquename":"SJAG_03753:allele-1"},"SJAG_04009:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04009","name":"ste11delta","uniquename":"SJAG_04009:allele-1"},"SJAG_04551:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04551","name":"pmk1delta","uniquename":"SJAG_04551:allele-1"},"SJAG_04777:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04777","name":"win1delta","uniquename":"SJAG_04777:allele-1"}},"annotation_curators":[{"annotation_count":38,"community_curator":true,"file_name":null,"file_type":null,"name":"Sho Okamoto","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-11-18","authors":"Nozaki S, Furuya K, Niki H","authors_abbrev":"Nozaki S et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2022-11-18 13:44:52","canto_curator_name":"Sho Okamoto","canto_curator_role":"community","canto_first_approved_date":"2022-11-18 13:44:52","canto_session_key":"18862c3d67da0cb0","canto_session_submitted_date":"2022-11-18 13:44:26","canto_triage_status":"Curatable","citation":"FEMS Yeast Res 2018 06 01;18(4)","cv_annotations":{"single_locus_phenotype":[{"annotations":[115423],"is_not":false,"summary":null,"term":"FYPO:0007773"},{"annotations":[115406,115407,115416,115438,115439],"is_not":false,"summary":null,"term":"FYPO:0007789"},{"annotations":[115435],"is_not":false,"summary":null,"term":"FYPO:0000584"},{"annotations":[115405,115409,115413],"is_not":false,"summary":null,"term":"FYPO:0001355"},{"annotations":[115437],"is_not":false,"summary":null,"term":"FYPO:0007790"},{"annotations":[115404,115410,115411,115415,115418,115420,115421,115434,115436],"is_not":false,"summary":null,"term":"FYPO:0000280"},{"annotations":[115412,115417,115419,115422,115424,115425,115426,115427,115428,115429,115430,115431,115432,115433],"is_not":false,"summary":null,"term":"FYPO:0000124"},{"annotations":[115403,115408,115414,115440],"is_not":false,"summary":null,"term":"FYPO:0002380"}]},"doi":"10.1093/femsyr/foy031","gene_count":17,"genes_by_uniquename":{"SJAG_00514":null,"SJAG_00993":null,"SJAG_01181":null,"SJAG_01718":null,"SJAG_01794":null,"SJAG_02342":null,"SJAG_02379":null,"SJAG_02486":null,"SJAG_02592":null,"SJAG_02819":null,"SJAG_02923":null,"SJAG_03384":null,"SJAG_03453":null,"SJAG_03753":null,"SJAG_04009":null,"SJAG_04551":null,"SJAG_04777":null},"genotypes_by_uniquename":{"byr1delta":{"display_name":"byr1delta","display_uniquename":"byr1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00993:allele-1","expression":"Null"}]}]},"byr2delta":{"display_name":"byr2delta","display_uniquename":"byr2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01718:allele-1","expression":"Null"}]}]},"efc25delta":{"display_name":"efc25delta","display_uniquename":"efc25delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02819:allele-1","expression":"Null"}]}]},"gap1delta":{"display_name":"gap1delta","display_uniquename":"gap1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02379:allele-1","expression":"Null"}]}]},"mkh1delta":{"display_name":"mkh1delta","display_uniquename":"mkh1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03753:allele-1","expression":"Null"}]}]},"pek1delta":{"display_name":"pek1delta","display_uniquename":"pek1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01181:allele-1","expression":"Null"}]}]},"pmk1delta":{"display_name":"pmk1delta","display_uniquename":"pmk1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-1","expression":"Null"}]}]},"ras1delta":{"display_name":"ras1delta","display_uniquename":"ras1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03453:allele-1","expression":"Null"}]}]},"scd1delta":{"display_name":"scd1delta","display_uniquename":"scd1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00514:allele-1","expression":"Null"}]}]},"scd2delta":{"display_name":"scd2delta","display_uniquename":"scd2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01794:allele-1","expression":"Null"}]}]},"spk1delta":{"display_name":"spk1delta","display_uniquename":"spk1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02923:allele-1","expression":"Null"}]}]},"ste11delta":{"display_name":"ste11delta","display_uniquename":"ste11delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04009:allele-1","expression":"Null"}]}]},"ste6delta":{"display_name":"ste6delta","display_uniquename":"ste6delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02486:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]},"win1delta":{"display_name":"win1delta","display_uniquename":"win1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04777:allele-1","expression":"Null"}]}]},"wis1delta":{"display_name":"wis1delta","display_uniquename":"wis1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02342:allele-1","expression":"Null"}]}]},"wis4delta":{"display_name":"wis4delta","display_uniquename":"wis4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03384:allele-1","expression":"Null"}]}]}},"ltp_gene_count":17,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2018","pubmed_entrez_date":"2018-03-23","pubmed_publication_date":"01 06 2018","terms_by_termid":{"FYECO:0000137":null,"FYPO:0000124":null,"FYPO:0000280":null,"FYPO:0000584":null,"FYPO:0001355":null,"FYPO:0002380":null,"FYPO:0007773":null,"FYPO:0007789":null,"FYPO:0007790":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null},"title":"The Ras1-Cdc42 pathway is involved in hyphal development of Schizosaccharomyces japonicus.","uniquename":"PMID:29566183"}


id: GO_REF:0000069
data:
  {"abstract":"We have created a standard template for classes describing the transmembrane transport of a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom template is \"GO:0055085 and 'transports or maintains localization of' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of transmembrane transport of a chemical as biological process in the Gene Ontology","uniquename":"GO_REF:0000069"}


id: GO_REF:0000101
data:
  {"abstract":"This reference is used to describe functional annotations transferred from one or more reference (\"source\") organisms to a newly annotated (\"target\") organism on the basis of ortholog cluster membership. In detail, predicted (e.g. by AUGUSTUS, see doi:10.1186/1471-2105-7-62) or transferred (e.g. via RATT, see doi:10:1093/nar/gkg1268) gene models in the target genome are translated and processed by OrthoMCL 1.4 together with reference protein sequences to produce clusters of gene products derived from orthologous genes. For each cluster, GO terms are automatically transferred from source products to the target gene products if they are experimentally verified (IDA (ECO:0000314), IMP (ECO:0000315), IPI (ECO:0000353), IGI (ECO:0000316), (EXP ECO:0000269). They are tagged with the ISO evidence code and the \"with/from\" is populated with the source feature references (e.g. \"GeneDB:LmjF.28.0960\"). OrthoMCL runs are done using the parameterization suggested in the OrthoMCL algorithm document (blastall -F 'm S' -e 1e-5).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Sascha Steinbiss, GeneDB curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Automated transfer of experimentally-verified GO annotation data to close orthologs","uniquename":"GO_REF:0000101"}


id: GO_REF:0000052
data:
  {"abstract":"GO Cellular Component terms are manually assigned by curators studying high resolution confocal microscopy images of immunohistochemically stained tissue. The methodology uses antibody-based proteomics which combines high-throughput generation of affinity-purified antibodies with protein profiling in a variety of cells and tissues. Further information on the annotation methods can be found at http://www.proteinatlas.org/about/assays+annotation <br>Annotations are only exported to the GO Consortium if the localizations are supported by literature, according to the following validation grading:<br>Supportive - Subcellular localization supported by literature.<br>1) One/multiple localizations supported by literature.<br>2) Multiple localizations partly supported (at least one) by literature.<br>3) One/multiple localizations in cytoplasm (i.e. Golgi, mitochondria, ER etc) with literature supporting cytoplasmic localization. <br>Prior to February 2013, all Human Protein Atlas annotations were referenced by PMID:18029348 (Barbe et al. 2008 Mol. Cell Proteomics. 7:499-508), a paper describing the protein localization pilot study and methodology used by the Human Protein Atlas. However, it has been decided that these annotations are more correctly described by a GO reference.<br>Resource URL: http://www.proteinatlas.org <br>Protein subcellular localization images can be viewed on the Human Protein Atlas website, e.g. http://www.proteinatlas.org/ENSG00000175899/summary#ifcelline","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Human Protein Atlas","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Gene Ontology annotation based on curation of immunofluorescence data","uniquename":"GO_REF:0000052"}


id: PMID:34198697
data:
  {"abstract":"Mitogen activated protein kinase (MAPK) signaling pathways execute essential functions in eukaryotic organisms by transducing extracellular stimuli into adaptive cellular responses. In the fission yeast model  Schizosaccharomyces pombe  the cell integrity pathway (CIP) and its core effector, MAPK Pmk1, play a key role during regulation of cell integrity, cytokinesis, and ionic homeostasis.  Schizosaccharomyces japonicus , another fission yeast species, shows remarkable differences with respect to  S. pombe , including a robust yeast to hyphae dimorphism in response to environmental changes. We show that the CIP MAPK module architecture and its upstream regulators, PKC orthologs Pck1 and Pck2, are conserved in both fission yeast species. However, some of  S. pombe 's CIP-related functions, such as cytokinetic control and response to glucose availability, are regulated differently in  S. japonicus.  Moreover, Pck1 and Pck2 antagonistically regulate  S. japonicus  hyphal differentiation through fine-tuning of Pmk1 activity. Chimeric MAPK-swapping experiments revealed that  S. japonicus  Pmk1 is fully functional in  S. pombe , whereas  S. pombe  Pmk1 shows a limited ability to execute CIP functions and promote  S. japonicus  mycelial development. Our findings also suggest that a modified N-lobe domain secondary structure within  S. japonicus  Pmk1 has a major influence on the CIP signaling features of this evolutionarily diverged fission 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21:32:21","canto_session_key":"0ba747685c452996","canto_session_submitted_date":"2021-09-14 17:59:01","canto_triage_status":"Curatable","citation":"J Fungi (Basel) 2021 Jun 14;7(6)","cv_annotations":{"PSI-MOD":[{"annotations":[115577,115578,115579],"is_not":false,"summary":null,"term":"MOD:00696"}],"cellular_component":[{"annotations":[115576],"is_not":false,"summary":null,"term":"GO:0005737"},{"annotations":[115575],"is_not":false,"summary":null,"term":"GO:0005634"}],"multi_locus_phenotype":[{"annotations":[115593],"is_not":false,"summary":null,"term":"FYPO:0007780"}],"single_locus_phenotype":[{"annotations":[115591,115599],"is_not":false,"summary":null,"term":"FYPO:0002678"},{"annotations":[115598],"is_not":false,"summary":null,"term":"FYPO:0002033"},{"annotations":[115580,115592,115596,115601,115604],"is_not":false,"summary":null,"term":"FYPO:0007776"},{"annotations":[115581,115597,115602,115605],"is_not":false,"summary":null,"term":"FYPO:0007780"},{"annotations":[115590,115594],"is_not":false,"summary":null,"term":"FYPO:0001838"},{"annotations":[115585],"is_not":false,"summary":null,"term":"FYPO:0007775"},{"annotations":[115586],"is_not":false,"summary":null,"term":"FYPO:0007779"},{"annotations":[115587],"is_not":false,"summary":null,"term":"FYPO:0002680"},{"annotations":[115584],"is_not":false,"summary":null,"term":"FYPO:0001038"},{"annotations":[115572],"is_not":false,"summary":null,"term":"FYPO:0004295"},{"annotations":[115582],"is_not":false,"summary":null,"term":"FYPO:0005152"},{"annotations":[115574,115589,115595,115600,115603],"is_not":false,"summary":null,"term":"FYPO:0007521"},{"annotations":[115573,115588],"is_not":false,"summary":null,"term":"FYPO:0000079"},{"annotations":[115583],"is_not":false,"summary":null,"term":"FYPO:0007522"}]},"doi":"10.3390/jof7060482","gene_count":4,"genes_by_uniquename":{"SJAG_00610":null,"SJAG_01787":null,"SJAG_02592":null,"SJAG_04551":null},"genotypes_by_uniquename":{"Pmk1Sj(ins82-105)-82-NITCIYDLDIIINPYNFNEVYIYEE-105-amino_acid_insertion-expression-not_assayed_or_wild_type":{"display_name":"Pmk1Sj(ins82-105)(82-NITCIYDLDIIINPYNFNEVYIYEE-105)","display_uniquename":"Pmk1Sj(ins82-105)-82-NITCIYDLDIIINPYNFNEVYIYEE-105-amino_acid_insertion-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-2","expression":"Not 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pmk1delta","display_uniquename":"pck1delta__pmk1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01787:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-1","expression":"Null"}]}]},"pck2delta":{"display_name":"pck2delta","display_uniquename":"pck2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00610:allele-1","expression":"Null"}]}]},"pmk1delta":{"display_name":"pmk1delta","display_uniquename":"pmk1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]}},"ltp_gene_count":4,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-07-02","pubmed_publication_date":"14 Jun 2021","terms_by_termid":{"FYECO:0000207":null,"FYECO:0000314":null,"FYPO:0000079":null,"FYPO:0001038":null,"FYPO:0001838":null,"FYPO:0002033":null,"FYPO:0002678":null,"FYPO:0002680":null,"FYPO:0004295":null,"FYPO:0005152":null,"FYPO:0007521":null,"FYPO:0007522":null,"FYPO:0007775":null,"FYPO:0007776":null,"FYPO:0007779":null,"FYPO:0007780":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"GO:0005634":null,"GO:0005737":null,"GO:0036460":null,"GO:0042149":null,"GO:0071475":null,"GO:0072690":null,"MOD:00696":null},"title":"Specific Functional Features of the Cell Integrity MAP Kinase Pathway in the Dimorphic Fission Yeast  Schizosaccharomyces japonicus .","uniquename":"PMID:34198697"}


id: GO_REF:0000094
data:
  {"abstract":"We have created a standard template for classes describing the development of a metazoan structure as a biological process. The underlying equivalence axiom template is \"'anatomical structure development' and 'results in development of' some E\", where E is a anatomical entity (UBERON:0001062).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of metazoan development as biological process in the Gene Ontology","uniquename":"GO_REF:0000094"}


id: GO_REF:0000027
data:
  {"abstract":"This GO reference describes the criteria used in assigning the evidence code of ISS via BLAST searches to annotate gene products from PAMGO_GAT. Standard BLASTP from NCBI was used (http://www.ncbi.nih.gov/blast) to query the non-redundant (NR) database. Hits are considered to be significant if the E-value is at or less than 10^-4. All other parameters are default according to http://www.ncbi.nih.gov/blast.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"PAMGO_GAT curators","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"BLAST search criteria for ISS assignment in PAMGO_GAT","uniquename":"GO_REF:0000027"}


id: PMID:26457121
data:
  {"abstract":"Transposable elements (TEs) are common constituents of centromeres. However, it is not known what causes this relationship. Schizosaccharomyces japonicus contains 10 families of Long Terminal Repeat (LTR)-retrotransposons and these elements cluster in centromeres and telomeres. In the related yeast, Schizosaccharomyces pombe LTR-retrotransposons Tf1 and Tf2 are distributed in the promoter regions of RNA pol II transcribed genes. Sequence analysis of TEs indicates that Tj1 of S. japonicus is related to Tf1 and Tf2, and uses the same mechanism of self-primed reverse transcription. Thus, we wondered why these related retrotransposons localized in different regions of the genome.\nTo characterize the integration behavior of Tj1 we expressed it in S. pombe. We found Tj1 was active and capable of generating de novo integration in the chromosomes of S. pombe. The expression of Tj1 is similar to Type C retroviruses in that a stop codon at the end of Gag must be present for efficient integration. 17 inserts were sequenced, 13 occurred within 12 bp upstream of tRNA genes and 3 occurred at other RNA pol III transcribed genes. The link between Tj1 integration and RNA pol III transcription is reminiscent of Ty3, an LTR-retrotransposon of Saccharomyces cerevisiae that interacts with TFIIIB and integrates upstream of tRNA genes.\nThe integration of Tj1 upstream of tRNA genes and the centromeric clustering of tRNA genes in S. japonicus demonstrate that the clustering of this TE in centromere sequences is due to a unique pattern of integration.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Guo Y, Singh PK, Levin HL","authors_abbrev":"Guo Y et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Mob DNA 2015;6:19","cv_annotations":{},"doi":"10.1186/s13100-015-0048-2","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-10-13","pubmed_publication_date":"2015","terms_by_termid":{},"title":"A long terminal repeat retrotransposon of Schizosaccharomyces japonicus integrates upstream of RNA pol III transcribed genes.","uniquename":"PMID:26457121"}


id: GO_REF:0000113
data:
  {"abstract":"The TFClass (http://tfclass.bioinf.med.uni-goettingen.de/index.jsf) database provides a comprehensive classification of mammalian DNA binding transcription factors (DbTFs) based on their DNA binding domains (DBDs) (PMID:29087517). TFClass classifies mammalian DbTFs by a five-level classification in which the four highest levels represent groups defined by structural and sequence similarities (superclass, class, family, subfamily, and genera) (more details at http://www.edgar-wingender.de/TFClass_schema.html). This classification is based on the combination of background knowledge of the molecular structural features of DBDs (PMID:9340487, PMID:23427989) and phylogenetic trees constructed via multiple sequence alignment with hierarchical clustering of manually validated DBDs and/or full-length protein sequences retrieved from UniProt (PMID:23427989, PMID:23180794, PMID:23427989). ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Marcio Luis Acencio (1), George Georghiou (2), Sandra Orchard (2), Liv Thommensen (1), Martin Kuiper (1) and Astrid Lægreid (1). (1) Norwegian University of Science and Technology (NTNU), Trondheim, Norway; (2) European Bioinformatics Institute (EBI), Hinxton, Cambridgeshire, United Kingdom","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Gene Ontology annotation of human sequence-specific DNA binding transcription factors (DbTFs) based on the TFClass database","uniquename":"GO_REF:0000113"}


id: PMID:26896847
data:
  {"abstract":"Evolution provides the unifying framework with which to understand biology. The coherent investigation of genic and genomic data often requires comparative genomics analyses based on whole-genome alignments, sets of homologous genes and other relevant datasets in order to evaluate and answer evolutionary-related questions. However, the complexity and computational requirements of producing such data are substantial: this has led to only a small number of reference resources that are used for most comparative analyses. The Ensembl comparative genomics resources are one such reference set that facilitates comprehensive and reproducible analysis of chordate genome data. Ensembl computes pairwise and multiple whole-genome alignments from which large-scale synteny, per-base conservation scores and constrained elements are obtained. Gene alignments are used to define Ensembl Protein Families, GeneTrees and homologies for both protein-coding and non-coding RNA genes. These resources are updated frequently and have a consistent informatics infrastructure and data presentation across all supported species. Specialized web-based visualizations are also available including synteny displays, collapsible gene tree plots, a gene family locator and different alignment views. The Ensembl comparative genomics infrastructure is extensively reused for the analysis of non-vertebrate species by other projects including Ensembl Genomes and Gramene and much of the information here is relevant to these projects. The consistency of the annotation across species and the focus on vertebrates makes Ensembl an ideal system to perform and support vertebrate comparative genomic analyses. We use robust software and pipelines to produce reference comparative data and make it freely available. 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comparative genomics resources.","uniquename":"PMID:26896847"}


id: GO_REF:0000075
data:
  {"abstract":"We have created a standard template for classes describing the transport of a chemical entity (ChEBI) into a cellular component as a biological process. The underlying equivalence axiom template is \"GO:0006810 and 'has_target_end_location' some T and 'imports' some S\", where T is a cellular component and S is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of transport of a chemical into a cellular component as biological process in the Gene Ontology","uniquename":"GO_REF:0000075"}


id: PMID:36148799
data:
  {"abstract":"Tropomyosins are structurally conserved α-helical coiled-coil proteins that bind along the length of filamentous actin (F-actin) in fungi and animals. Tropomyosins play essential roles in the stability of actin filaments and in regulating myosin II contractility. Despite the crucial role of tropomyosin in actin cytoskeletal regulation, in vivo investigations of tropomyosin are limited, mainly due to the suboptimal live-cell imaging tools currently available. Here, we report on an mNeonGreen (mNG)-tagged tropomyosin, with native promoter and linker length configuration, that clearly reports tropomyosin dynamics in Schizosaccharomyces pombe (Cdc8), Schizosaccharomyces japonicus (Cdc8) and Saccharomyces cerevisiae (Tpm1 and Tpm2). We also describe a fluorescent probe to visualize mammalian tropomyosin (TPM2 isoform). Finally, we generated a camelid nanobody against S. pombe Cdc8, which mimics the localization of mNG-Cdc8 in vivo. Using these tools, we report the presence of tropomyosin in previously unappreciated patch-like structures in fission and budding yeasts, show flow of tropomyosin (F-actin) cables to the cytokinetic actomyosin ring and identify rearrangements of the actin cytoskeleton during mating. These powerful tools and strategies will aid better analyses of tropomyosin and F-actin cables in vivo.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":3,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-11-25","authors":"Hatano T, Lim TC, Billault-Chaumartin I, Dhar A, Gu Y, Massam-Wu T, Scott W, Adishesha S, Chapa-Y-Lazo B, Springall L, Sivashanmugam L, Mishima M, Martin SG, Oliferenko S, Palani S, Balasubramanian MK","authors_abbrev":"Hatano T et al.","canto_added_date":"2022-11-25 12:03:53","canto_annotation_status":"APPROVED","canto_approved_date":"2022-11-25 12:11:22","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2022-11-25 12:11:22","canto_session_key":"d572e8fc7f8a7a38","canto_session_submitted_date":"2022-11-25 12:11:07","canto_triage_status":"Curatable","citation":"J Cell Sci 2022 Sep 15;135(18)","cv_annotations":{"cellular_component":[{"annotations":[115609],"is_not":false,"summary":null,"term":"GO:0070648"},{"annotations":[115611],"is_not":false,"summary":null,"term":"GO:1990819"},{"annotations":[115610],"is_not":false,"summary":null,"term":"GO:0110085"}]},"doi":"10.1242/jcs.260288","gene_count":1,"genes_by_uniquename":{"SJAG_04887":null},"genotypes_by_uniquename":{},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-09-23","pubmed_publication_date":"15 Sep 2022","terms_by_termid":{"GO:0070648":null,"GO:0110085":null,"GO:1990819":null},"title":"mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells.","uniquename":"PMID:36148799"}


id: PMID:34353908
data:
  {"abstract":"Biosynthesis of sterols, which are key constituents of canonical eukaryotic membranes, requires molecular oxygen. Anaerobic protists and deep-branching anaerobic fungi are the only eukaryotes in which a mechanism for sterol-independent growth has been elucidated. In these organisms, tetrahymanol, formed through oxygen-independent cyclization of squalene by a squalene-tetrahymanol cyclase, acts as a sterol surrogate. This study confirms an early report [C. J. E. A. Bulder,  Antonie Van Leeuwenhoek , 37, 353-358 (1971)] that  Schizosaccharomyces japonicus  is exceptional among yeasts in growing anaerobically on synthetic media lacking sterols and unsaturated fatty acids. Mass spectrometry of lipid fractions of anaerobically grown  Sch. japonicus  showed the presence of hopanoids, a class of cyclic triterpenoids not previously detected in yeasts, including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22-ol. A putative gene in  Sch. japonicus  showed high similarity to bacterial squalene-hopene cyclase (SHC) genes and in particular to those of  Acetobacter  species. No orthologs of the putative  Sch. japonicus  SHC were found in other yeast species. Expression of the  Sch. japonicus  SHC gene ( Sjshc1 ) in  Saccharomyces cerevisiae  enabled hopanoid synthesis and stimulated anaerobic growth in sterol-free media, thus indicating that one or more of the hopanoids produced by SjShc1 could at least partially replace sterols. Use of hopanoids as sterol surrogates represents a previously unknown adaptation of eukaryotic cells to anaerobic growth. The fast anaerobic growth of  Sch. japonicus  in sterol-free media is an interesting trait for developing robust fungal cell factories for application in anaerobic industrial processes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bouwknegt J, Wiersma SJ, Ortiz-Merino RA, Doornenbal ESR, Buitenhuis P, Giera M, Müller C, Pronk JT","authors_abbrev":"Bouwknegt J et al.","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Proc Natl Acad Sci U S A 2021 Aug 10;118(32)","cv_annotations":{},"doi":"10.1073/pnas.2105225118","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-08-06","pubmed_publication_date":"10 Aug 2021","terms_by_termid":{},"title":"A squalene-hopene cyclase in  Schizosaccharomyces japonicus  represents a eukaryotic adaptation to sterol-limited anaerobic environments.","uniquename":"PMID:34353908"}


id: PMID:36058798
data:
  {"abstract":"Schizosaccharomyces japonicus is a dimorphic yeast, transiting between unicellular and hyphal growth. The glycoproteins of fission yeast contain, in addition to mannose (Man), a large number of galactose (Gal) residues. Previously, we reported that the cell-surface O-glycans of S. japonicus comprise mainly tri-saccharides (Gal-Man-Man) as a main component, in contrast to the tetra-saccharides observed in other Schizosaccharomyces species. Here we have investigated the function of cell-surface Gal residues in S. japonicus. Because disruption of gms1 + , encoding the UDP-Gal transporter required for galactomannan synthesis, abolishes cell-surface galactosylation in Schizosaccharomyces pombe, we constructed a deletion mutant of the homologous gene in S. japonicus gms1Δ [gms1 (S.j)] and determined the N- and O-linked oligosaccharide structures present on the cell surface. Disruption of gms1 (S.j) resulted in a complete lack of Gal on the cell surface, indicating that Gms1 plays an essential role in supplying UDP-Gal from the cytoplasm to the Golgi lumen. Analytical microscopy of gms1Δ demonstrated that the lack of cell-surface Gal did not affect cell growth or morphology during vegetative growth. However, hyphal development was blocked in gms1Δ, even in the presence of the topoisomerase I inhibitor camptothecin, which is known to induce hyphal differentiation in wild-type S. japonicus. Collectively, these findings show that Gal-containing oligosaccharides are required for cell wall integrity during filamentous growth in S. japonicus.","alleles_by_uniquename":{"SJAG_04697:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04697","name":"gms1delta","uniquename":"SJAG_04697:allele-1"}},"annotation_curators":[{"annotation_count":6,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-12-01","authors":"Fukunaga T, Ohashi T, Tanaka Y, Yoshimatsu T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Fukunaga T et al.","canto_added_date":"2022-11-25 12:12:27","canto_annotation_status":"APPROVED","canto_approved_date":"2022-12-01 10:35:53","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2022-12-01 10:35:53","canto_session_key":"465355706dc223a3","canto_session_submitted_date":"2022-11-25 12:49:07","canto_triage_status":"Curatable","citation":"J Biosci Bioeng 2022 Nov;134(5):384-392","cv_annotations":{"single_locus_phenotype":[{"annotations":[115088],"is_not":false,"summary":null,"term":"FYPO:0008029"},{"annotations":[115084],"is_not":false,"summary":null,"term":"FYPO:0000082"},{"annotations":[115087],"is_not":false,"summary":null,"term":"FYPO:0007776"},{"annotations":[115086],"is_not":false,"summary":null,"term":"FYPO:0007780"},{"annotations":[115083],"is_not":false,"summary":null,"term":"FYPO:0003727"},{"annotations":[115085],"is_not":false,"summary":null,"term":"FYPO:0000106"}]},"doi":"10.1016/j.jbiosc.2022.07.014","gene_count":1,"genes_by_uniquename":{"SJAG_04697":null},"genotypes_by_uniquename":{"gms1delta":{"display_name":"gms1delta","display_uniquename":"gms1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04697:allele-1","expression":"Null"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-09-04","pubmed_publication_date":"Nov 2022","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000005":null,"FYECO:0000126":null,"FYECO:0000137":null,"FYECO:0000314":null,"FYPO:0000082":null,"FYPO:0000106":null,"FYPO:0003727":null,"FYPO:0007776":null,"FYPO:0007780":null,"FYPO:0008029":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null},"title":"Galactosylation of cell-surface glycoprotein required for hyphal growth and cell wall integrity in Schizosaccharomyces japonicus.","uniquename":"PMID:36058798"}


id: GO_REF:0000107
data:
  {"abstract":"GO terms from a source species are projected onto one or more target species based on gene orthology obtained from Ensembl Compara. One-to-one, one-to-many and many-to-many orthology relations and anntations are transferred between orthologs that have at least a 40% peptide identity to each other. Only GO annotations with evidence codes ECO:0000314 (IDA), ECO:0000270 (IEP), ECO:0000316 (IGI), ECO:0000315 (IMP), and ECO:0000353 (IPI), or their descendants, are transferred; annotations with a 'NOT' qualifier are not transferred, and neither are annotations to GO:0005515 (protein binding). Annotations that are transferred using this method receive the evidence code ECO:0000265 (sequence orthology evidence used in automatic assertion), which maps up to the GO Inferred from Electronic Annotation (IEA) evidence code.  The model organism database identifier of the annotation source will be indicated in the 'With' column of the GOA association file.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GOA 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