Metalloprotease subunit of the 19S regulatory particle of the 26S proteasome lid; couples the deubiquitination and degradation of proteasome substrates; involved, independent of catalytic activity, in fission of mitochondria and peroxisomes; protein abundance increases in response to DNA replication stress
Zygosity: Heterozygous strain
fixedexpanded
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Top fitness defect scores for YFR004W deletion by condition
Download Fitness data (tab-delimited text) (excel) |
Correlation | pval | ORF | Gene | Zygosity | Description |
---|---|---|---|---|---|
0.282 | 4.84E-62 | YOR117W | RPT5 | het | One of six ATPases of the 19S regulatory particle of the 26S proteasome involved in the degradation of ubiquitinated substrates; recruited to the GAL1-10 promoter region upon induction of transcription; similar to human TBP1 |
0.236 | 1.29E-43 | YER021W | RPN3 | het | Essential, non-ATPase regulatory subunit of the 26S proteasome lid, similar to the p58 subunit of the human 26S proteasome; temperature-sensitive alleles cause metaphase arrest, suggesting a role for the proteasome in cell cycle control |
0.228 | 1.01E-40 | YDL007W | RPT2 | het | One of six ATPases of the 19S regulatory particle of the 26S proteasome involved in the degradation of ubiquitinated substrates; required for normal peptide hydrolysis by the core 20S particle |
0.224 | 4.33E-39 | YDL097C | RPN6 | het | Essential, non-ATPase regulatory subunit of the 26S proteasome lid; required for the assembly and activity of the 26S proteasome; the human homolog (S9 protein) partially rescues Rpn6p depletion; protein abundance increases in response to DNA replication stress |
0.219 | 1.11E-37 | YGL048C | RPT6 | het | ATPase of the 19S regulatory particle of the 26S proteasome; one of six ATPases of the regulatory particle; involved in the degradation of ubiquitinated substrates; bound by ubiquitin-protein ligases Ubr1p and Ufd4p; localized mainly to the nucleus throughout the cell cycle; protein abundance increases in response to DNA replication stress |
0.195 | 6.20E-30 | YDR427W | RPN9 | het | Non-ATPase regulatory subunit of the 26S proteasome; has similarity to putative proteasomal subunits in other species; null mutant is temperature sensitive and exhibits cell cycle and proteasome assembly defects; protein abundance increases in response to DNA replication stress |
0.193 | 1.74E-29 | YFR052W | RPN12 | het | Subunit of the 19S regulatory particle of the 26S proteasome lid; synthetically lethal with RPT1, which is an ATPase component of the 19S regulatory particle; physically interacts with Nob1p and Rpn3p; protein abundance increases in response to DNA replication stress |
0.192 | 4.56E-29 | YDL147W | RPN5 | het | Subunit of the COP9 signalosome (CSN) and non-ATPase regulatory subunit of the 26S proteasome lid, similar to mammalian p55 subunit and to another S. cerevisiae regulatory subunit, Rpn7p; Rpn5p is an essential protein |
0.145 | 3.53E-17 | YFR050C | PRE4 | het | Beta 7 subunit of the 20S proteasome |
0.143 | 8.61E-17 | YOR261C | RPN8 | het | Essential, non-ATPase regulatory subunit of the 26S proteasome; has similarity to the human p40 proteasomal subunit and to another S. cerevisiae regulatory subunit, Rpn11p |
0.142 | 1.92E-16 | YDR527W | RBA50 | het | Protein involved in transcription; interacts with RNA polymerase II subunits Rpb2p, Rpb3, and Rpb11p; has similarity to human RPAP1 |
0.141 | 3.24E-16 | YDR394W | RPT3 | het | One of six ATPases of the 19S regulatory particle of the 26S proteasome involved in the degradation of ubiquitinated substrates; substrate of N-acetyltransferase B |
0.136 | 2.79E-15 | YBL041W | PRE7 | het | Beta 6 subunit of the 20S proteasome |
0.126 | 2.67E-13 | YOR259C | RPT4 | het | One of six ATPases of the 19S regulatory particle of the 26S proteasome involved in degradation of ubiquitinated substrates; contributes preferentially to ERAD; required for spindle pole body duplication; mainly nuclear localization |
0.115 | 2.24E-11 | YOL038W | PRE6 | het | Alpha 4 subunit of the 20S proteasome; may replace alpha 3 subunit (Pre9p) under stress conditions to create a more active proteasomal isoform; GFP-fusion protein relocates from cytosol to the mitochondrial surface upon oxidative stress |