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RPT2 RPT2 RPN6 RPN6 RPN5 RPN5 RPT3 RPT3 RPN9 RPN9 RPN3 RPN3 RPN11 RPN11 UBP6 UBP6 RPN12 RPN12 RPT6 RPT6 RPN10 RPN10 RPT1 RPT1 RPN13 RPN13 RPT5 RPT5 RPT4 RPT4 RPN8 RPN8 RPN7 RPN7
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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RPT2ATPase of the 19S regulatory particle of the 26S proteasome; one of six ATPases of the regulatory particle; involved in the degradation of ubiquitinated substrates; required for normal peptide hydrolysis by the core 20S particle; N-myristoylation of Rpt2p at Gly2 is involved in regulating the proper intracellular distribution of proteasome activity by controlling the nuclear localization of the 26S proteasome. (437 aa)
RPN6Essential, 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. (434 aa)
RPN5Subunit of the CSN and 26S proteasome lid complexes; similar to mammalian p55 subunit and to another S. cerevisiae regulatory subunit, Rpn7p; Rpn5p is an essential protein; the COP9 signalosome is also known as the CSN. (445 aa)
RPT3ATPase of the 19S regulatory particle of the 26S proteasome; one of ATPases of the regulatory particle; involved in the degradation of ubiquitinated substrates; substrate of N-acetyltransferase B. (428 aa)
RPN9Non-ATPase regulatory subunit of the 26S proteasome; similar 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; relocalizes to the cytosol in response to hypoxia. (393 aa)
RPN3Essential 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. (523 aa)
RPN11Ubiquitin carboxyl-terminal hydrolase RPN11; Metalloprotease subunit of 19S regulatory particle; part of 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. (306 aa)
UBP6Ubiquitin-specific protease; situated in the base subcomplex of the 26S proteasome, releases free ubiquitin from branched polyubiquitin chains en bloc, rather than from the distal tip of the chain; negatively regulates degradation of ubiquitinated proteins by the proteasome; works in opposition to Hul5p polyubiquitin elongation activity; mutant has aneuploidy tolerance; human homolog UBP14 complements yeast null mutant. (499 aa)
RPN12Subunit 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. (274 aa)
RPT6ATPase 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. (405 aa)
RPN10Non-ATPase base subunit of the 19S RP of the 26S proteasome; N-terminus plays a role in maintaining the structural integrity of the regulatory particle (RP); binds selectively to polyubiquitin chains; homolog of the mammalian S5a protein. (268 aa)
RPT1ATPase of the 19S regulatory particle of the 26S proteasome; one of six ATPases of the regulatory particle; involved in the degradation of ubiquitinated substrates; required for optimal CDC20 transcription; interacts with Rpn12p and Ubr1p; mutant has aneuploidy tolerance. (467 aa)
RPN13Subunit of the 19S regulatory particle of the 26S proteasome lid; acts as a ubiquitin receptor for the proteasome; null mutants accumulate ubiquitinated Gcn4p and display decreased 26S proteasome stability; protein abundance increases in response to DNA replication stress; Belongs to the RPN13 family. (156 aa)
RPT5ATPase of the 19S regulatory particle of the 26S proteasome; one of six ATPases of the regulatory particle; involved in the degradation of ubiquitinated substrates; recruited to the GAL1-10 promoter region upon induction of transcription; similar to human TBP1. (434 aa)
RPT426S proteasome subunit RPT4; ATPase of the 19S regulatory particle of the 26S proteasome; one of six ATPases of the regulatory particle; involved in degradation of ubiquitinated substrates; contributes preferentially to ERAD; required for spindle pole body duplication; mainly nuclear localization. (437 aa)
RPN8Essential non-ATPase regulatory subunit of the 26S proteasome; has similarity to the human p40 proteasomal subunit and to another S. cerevisiae regulatory subunit, Rpn11p; Belongs to the peptidase M67A family. (338 aa)
RPN7Essential non-ATPase regulatory subunit of the 26S proteasome; similar to another S. cerevisiae regulatory subunit, Rpn5p, as well as to mammalian proteasome subunits. (429 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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