{
    "bcoid": "GLY_000750",
    "title": "Yeast Protein Function (UniProtKB)",
    "description": "The Yeast Protein Function (UniProtKB) dataset contains biological function annotation for yeast [taxid:559292] ...",
    "filename": "yeast_protein_function_uniprotkb.csv",
    "filetype": "csv",
    "categories": {
        "species": [
            "Saccharomyces cerevisiae S288C"
        ],
        "molecule": [
            "Protein"
        ],
        "tag": [
            "Protein Function"
        ],
        "file_type": [
            "csv"
        ],
        "status": [
            "Reviewed"
        ],
        "scope": [
            "internal"
        ]
    },
    "minitable": {
        "content": [
            [
                "Q03761-1...",
                "protein_xref..."
            ],
            [
                "Q03761-1...",
                "protein_xref..."
            ]
        ],
        "headers": [
            "uniprotkb_ca...",
            "xref_key..."
        ],
        "colwidth": [
            "40%",
            "20%"
        ]
    },
    "sampledata": {
        "type": "table",
        "data": [
            [
                {
                    "type": "string",
                    "label": "uniprotkb_canonical_ac"
                },
                {
                    "type": "string",
                    "label": "xref_key"
                },
                {
                    "type": "string",
                    "label": "xref_id"
                },
                {
                    "type": "string",
                    "label": "annotation"
                }
            ],
            [
                "Q03761-1",
                "protein_xref_uniprotkb_fun",
                "Q03761",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "10788514",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "9674426",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "12052880",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "9695952",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "11473260",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "12516863",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "11295558",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "10026213",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "11238921",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q03761-1",
                "protein_xref_pubmed",
                "12138208",
                "Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus."
            ],
            [
                "Q06108-1",
                "protein_xref_uniprotkb_fun",
                "Q06108",
                "Positive regulator of FPS1 glycerol channel required for the glycerol efflux."
            ],
            [
                "Q06108-1",
                "protein_xref_pubmed",
                "19956799",
                "Positive regulator of FPS1 glycerol channel required for the glycerol efflux."
            ],
            [
                "Q06108-1",
                "protein_xref_pubmed",
                "12829295",
                "Positive regulator of FPS1 glycerol channel required for the glycerol efflux."
            ],
            [
                "Q06109-1",
                "protein_xref_uniprotkb_fun",
                "Q06109",
                "Required for respiratory activity and maintenance and expression of the mitochondrial genome."
            ],
            [
                "Q06109-1",
                "protein_xref_pubmed",
                "19751518",
                "Required for respiratory activity and maintenance and expression of the mitochondrial genome."
            ],
            [
                "Q03760-1",
                "protein_xref_uniprotkb_fun",
                "Q03760",
                "Involved in the nuclear retention of improperly spliced pre-mRNAs."
            ],
            [
                "Q03760-1",
                "protein_xref_pubmed",
                "16162818",
                "Involved in the nuclear retention of improperly spliced pre-mRNAs."
            ],
            [
                "Q06102-1",
                "protein_xref_uniprotkb_fun",
                "Q06102",
                "RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB."
            ],
            [
                "Q06102-1",
                "protein_xref_pubmed",
                "12626716",
                "RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB."
            ],
            [
                "Q05635-1",
                "protein_xref_uniprotkb_fun",
                "Q05635",
                "Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes."
            ],
            [
                "Q05635-1",
                "protein_xref_pubmed",
                "16193328",
                "Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes."
            ],
            [
                "Q06106-1",
                "protein_xref_uniprotkb_fun",
                "Q06106",
                "Involved in pre-rRNA processing. Required for maintaining steady-state levels of 40S ribosomal subunit. Required for the initial processing of pre-rRNA at the A0 to A2 sites, leading to the processing of the 23S pre-rRNA intermediate to the 18S rRNA."
            ],
            [
                "Q06106-1",
                "protein_xref_pubmed",
                "11884397",
                "Involved in pre-rRNA processing. Required for maintaining steady-state levels of 40S ribosomal subunit. Required for the initial processing of pre-rRNA at the A0 to A2 sites, leading to the processing of the 23S pre-rRNA intermediate to the 18S rRNA."
            ],
            [
                "P30619-1",
                "protein_xref_uniprotkb_fun",
                "P30619",
                "Involved in the final stage of protein secretion."
            ],
            [
                "Q06104-1",
                "protein_xref_uniprotkb_fun",
                "Q06104",
                "Component of the Golgi/endosome-localized DSC E3 ubiquitin ligase complex involved in the targeting of the DSC complex to the Golgi apparatus and endosome membranes via the AP3 pathway to ubiquinate Golgi/endosome membrane proteins (PubMed:29355480). Competes with VLD1 to determine the subcellular localizations of the DSC complex (PubMed:29355480). May be required for cell cycle progression (PubMed:12829295)."
            ],
            [
                "Q06104-1",
                "protein_xref_pubmed",
                "29355480",
                "Component of the Golgi/endosome-localized DSC E3 ubiquitin ligase complex involved in the targeting of the DSC complex to the Golgi apparatus and endosome membranes via the AP3 pathway to ubiquinate Golgi/endosome membrane proteins (PubMed:29355480). Competes with VLD1 to determine the subcellular localizations of the DSC complex (PubMed:29355480). May be required for cell cycle progression (PubMed:12829295)."
            ],
            [
                "Q06104-1",
                "protein_xref_pubmed",
                "12829295",
                "Component of the Golgi/endosome-localized DSC E3 ubiquitin ligase complex involved in the targeting of the DSC complex to the Golgi apparatus and endosome membranes via the AP3 pathway to ubiquinate Golgi/endosome membrane proteins (PubMed:29355480). Competes with VLD1 to determine the subcellular localizations of the DSC complex (PubMed:29355480). May be required for cell cycle progression (PubMed:12829295)."
            ],
            [
                "P32378-1",
                "protein_xref_uniprotkb_fun",
                "P32378",
                "Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate."
            ],
            [
                "P32378-1",
                "protein_xref_pubmed",
                "1740455",
                "Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate."
            ],
            [
                "P32378-1",
                "protein_xref_uniprotkb_fun",
                "MF_03189",
                "Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate."
            ],
            [
                "P40554-1",
                "protein_xref_uniprotkb_fun",
                "P40554",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "19151091",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "10713047",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "14555475",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "19145231",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "19017811",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "18755837",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "21209336",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "14551258",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40554-1",
                "protein_xref_pubmed",
                "18664566",
                "Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth."
            ],
            [
                "P40555-1",
                "protein_xref_uniprotkb_fun",
                "P40555",
                "Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC). During the base subcomplex assembly is part of a NAS2:RPT4:RPT5 module; NAS2 is released during the further base assembly process."
            ],
            [
                "P40555-1",
                "protein_xref_pubmed",
                "19446322",
                "Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC). During the base subcomplex assembly is part of a NAS2:RPT4:RPT5 module; NAS2 is released during the further base assembly process."
            ],
            [
                "P39970-1",
                "protein_xref_uniprotkb_fun",
                "P39970",
                "Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities."
            ],
            [
                "P39970-1",
                "protein_xref_pubmed",
                "16464826",
                "Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities."
            ],
            [
                "P39970-1",
                "protein_xref_pubmed",
                "14966276",
                "Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities."
            ],
            [
                "P39970-1",
                "protein_xref_pubmed",
                "10825197",
                "Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities."
            ],
            [
                "P39970-1",
                "protein_xref_pubmed",
                "12051917",
                "Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities."
            ],
            [
                "P48562-1",
                "protein_xref_uniprotkb_fun",
                "P48562",
                "Involved in budding and cytokinesis."
            ],
            [
                "P39976-1",
                "protein_xref_uniprotkb_fun",
                "P39976",
                "Catalyzes the reversible oxidation of (R)-2-hydroxyglutarate to 2-oxoglutarate coupled to reduction of pyruvate to (R)-lactate. Can also use oxaloacetate as electron acceptor instead of pyruvate producing (R)-malate."
            ],
            [
                "P39976-1",
                "protein_xref_pubmed",
                "26774271",
                "Catalyzes the reversible oxidation of (R)-2-hydroxyglutarate to 2-oxoglutarate coupled to reduction of pyruvate to (R)-lactate. Can also use oxaloacetate as electron acceptor instead of pyruvate producing (R)-malate."
            ],
            [
                "P48564-1",
                "protein_xref_uniprotkb_fun",
                "P48564",
                "Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression."
            ],
            [
                "P48564-1",
                "protein_xref_pubmed",
                "25683707",
                "Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression."
            ],
            [
                "P40552-1",
                "protein_xref_uniprotkb_fun",
                "P40552",
                "Component of the cell wall. Required for anaerobic growth."
            ],
            [
                "P40552-1",
                "protein_xref_pubmed",
                "11292809",
                "Component of the cell wall. Required for anaerobic growth."
            ],
            [
                "P10659-1",
                "protein_xref_uniprotkb_fun",
                "P10659",
                "Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate."
            ],
            [
                "P10659-1",
                "protein_xref_pubmed",
                "3316224",
                "Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate."
            ],
            [
                "Q03441-1",
                "protein_xref_uniprotkb_fun",
                "Q03441",
                "Required for sporulation where it is believed to have a role in meiotic nuclear division."
            ],
            [
                "Q03441-1",
                "protein_xref_pubmed",
                "12586695",
                "Required for sporulation where it is believed to have a role in meiotic nuclear division."
            ],
            [
                "P38132-1",
                "protein_xref_uniprotkb_fun",
                "P38132",
                "Acts as a component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity."
            ],
            [
                "P38132-1",
                "protein_xref_pubmed",
                "19910535",
                "Acts as a component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity."
            ],
            [
                "P38132-1",
                "protein_xref_pubmed",
                "19896182",
                "Acts as a component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity."
            ],
            [
                "P39979-1",
                "protein_xref_uniprotkb_fun",
                "P39979",
                "N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine (PubMed:23775086). Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated (PubMed:15375647). D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids (PubMed:10600387, PubMed:16362288)."
            ],
            [
                "P39979-1",
                "protein_xref_pubmed",
                "16362288",
                "N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine (PubMed:23775086). Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated (PubMed:15375647). D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids (PubMed:10600387, PubMed:16362288)."
            ],
            [
                "P39979-1",
                "protein_xref_pubmed",
                "23775086",
                "N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine (PubMed:23775086). Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated (PubMed:15375647). D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids (PubMed:10600387, PubMed:16362288)."
            ],
            [
                "P39979-1",
                "protein_xref_pubmed",
                "15375647",
                "N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine (PubMed:23775086). Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated (PubMed:15375647). D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids (PubMed:10600387, PubMed:16362288)."
            ],
            [
                "P39979-1",
                "protein_xref_pubmed",
                "10600387",
                "N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine (PubMed:23775086). Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated (PubMed:15375647). D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids (PubMed:10600387, PubMed:16362288)."
            ],
            [
                "P40558-1",
                "protein_xref_uniprotkb_fun",
                "P40558",
                "Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:12970194, PubMed:15660135, PubMed:17401378). Required for maturation of extramitochondrial Fe-S proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378, PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:17401378, PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766). Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export (PubMed:15660135)."
            ],
            [
                "P40558-1",
                "protein_xref_uniprotkb_fun",
                "MF_03039",
                "Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:12970194, PubMed:15660135, PubMed:17401378). Required for maturation of extramitochondrial Fe-S proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378, PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:17401378, PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766). Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export (PubMed:15660135)."
            ],
            [
                "P40558-1",
                "protein_xref_pubmed",
                "22362766",
                "Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:12970194, PubMed:15660135, PubMed:17401378). Required for maturation of extramitochondrial Fe-S proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378, PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:17401378, PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766). Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export (PubMed:15660135)."
            ],
            [
                "P40558-1",
                "protein_xref_pubmed",
                "12970194",
                "Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:12970194, PubMed:15660135, PubMed:17401378). Required for maturation of extramitochondrial Fe-S proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378, PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:17401378, PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766). Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export (PubMed:15660135)."
            ],
            [
                "P40558-1",
                "protein_xref_pubmed",
                "15660135",
                "Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:12970194, PubMed:15660135, PubMed:17401378). Required for maturation of extramitochondrial Fe-S proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378, PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:17401378, PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766). Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export (PubMed:15660135)."
            ],
            [
                "P40558-1",
                "protein_xref_pubmed",
                "31040179",
                "Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:12970194, PubMed:15660135, PubMed:17401378). Required for maturation of extramitochondrial Fe-S proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378, PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:17401378, PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766). Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export (PubMed:15660135)."
            ],
            [
                "P40558-1",
                "protein_xref_pubmed",
                "17401378",
                "Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:12970194, PubMed:15660135, PubMed:17401378). Required for maturation of extramitochondrial Fe-S proteins (PubMed:12970194, PubMed:15660135, PubMed:17401378, PubMed:22362766, PubMed:31040179). The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:17401378, PubMed:22362766). Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35 (PubMed:22362766). Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export (PubMed:15660135)."
            ],
            [
                "P40559-1",
                "protein_xref_uniprotkb_fun",
                "P40559",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "P40559-1",
                "protein_xref_pubmed",
                "15265867",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "P40559-1",
                "protein_xref_pubmed",
                "11311145",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "P40559-1",
                "protein_xref_pubmed",
                "9788876",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "P40559-1",
                "protein_xref_pubmed",
                "9560389",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "P40559-1",
                "protein_xref_pubmed",
                "17452534",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "P40559-1",
                "protein_xref_pubmed",
                "15689497",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "P40559-1",
                "protein_xref_pubmed",
                "15691741",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "P40559-1",
                "protein_xref_pubmed",
                "9265642",
                "Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth."
            ],
            [
                "Q03195-1",
                "protein_xref_uniprotkb_fun",
                "Q03195",
                "Component of the multifactor complex (MFC) involved in translation initiation. Required for the binding of MFC to the 40S ribosome. Required for the processing and nuclear export of the 60S and 40S ribosomal subunits."
            ]
        ]
    },
    "readme": "Name\n   - Yeast Protein Function (UniProtKB)\n\nVersion\n   - v-2.4.1\n\nCreated on\n  - 2022-08-30T14:58:43.098400\n\nModified on\n   - 2023-09-11T18:59:49\n\nCreated by\n   - Jeet Vora [jeetvora@gwu.edu], Robel Kahsay [rykahsay@gwu.edu], Karina Martinez [karinamartinez@gwu.edu], Jingyue Wu [jingyue.wu@email.gwu.edu], Luke Johnson [luke.johnson@email.gwu.edu], Urnisha Bhuiyan [sbhuiyan28@email.gwu.edu], Cyrus Au-Yeung [cyruschauyeung@gwu.edu], Jingyue Wu [jingyue.wu@email.gwu.edu]\n\nAuthors\n   - Maria Martin [martin@ebi.ac.uk], Preethi Vasudev [pvasudev@ebi.ac.uk]\n\nChecksum\n   - \n\nUsability Domain\n   - The Yeast Protein Function (UniProtKB) dataset contains biological function annotation for yeast [taxid:559292] protein accessions from the UniProtKB database. If you use this dataset please provide proper attribution to EMBL-EBI-UniProtKB and GlyGen. \n\nDescription Domain\n   Keywords\n   - protein function\n   - UniProtKB\n\n   Pipeline Steps\n   - Step-1: The script loads the UniProtKB function annotations triplestore containing triples from nt file and extracts the data as a csv dataset. \n\nExecution Domain\n   Scripts   - https://github.com/glygener/glygen-backend-integration/blob/master/dataset-maker/make-protein-dataset.py\n\n\n   Software Prerequisites\n      Name: Python\n      Version: 2.7.5\n      URI: https://www.python.org/download/releases/2.7.5/\n\nI/O Domain\n   Input Subdomain\n      Name: uniprot-proteome-saccharomyces-cerevisiae.nt\n      URI: https:/data.glygen.org/ln2downloads/ebi/2024_02_19/uniprot-proteome-saccharomyces-cerevisiae.nt\n   Output Subdomain\n      Name: yeast_protein_function_uniprotkb.csv\n      URI: https:/data.glygen.org/ln2releases/data/v-2.4.1/reviewed/yeast_protein_function_uniprotkb.csv\n      Name: yeast_protein_function_uniprotkb.stat.csv\n      URI: https:/data.glygen.org/ln2releases/data/v-2.4.1/reviewed/yeast_protein_function_uniprotkb.stat.csv\n\nFields\n      Name: \"uniprotkb_canonical_ac\"\n     Description: \"\"\n      Unique Values: \"4846\"\n      Name: \"xref_key\"\n     Description: \"Source key associated to the  xref_id\"\n      Unique Values: \"2\"\n      Name: \"xref_id\"\n     Description: \"ID of the X-ref\"\n      Unique Values: \"12117\"\n      Name: \"annotation\"\n     Description: \"Function annotation from UniProtKB|RefSeq database\"\n      Unique Values: \"4052\"",
    "downloadurl": "/ln2data/releases/data/v-2.4.1/reviewed/yeast_protein_function_uniprotkb.csv"
}