P32565 · RPN2_YEAST
- Protein26S proteasome regulatory subunit RPN2
- GeneRPN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids945 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Miscellaneous
Present with 4750 molecules/cell in log phase SD medium.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | proteasome complex | |
Cellular Component | proteasome regulatory particle, base subcomplex | |
Cellular Component | proteasome storage granule | |
Molecular Function | enzyme regulator activity | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | proteasome assembly | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | regulation of protein catabolic process | |
Biological Process | ubiquitin-dependent protein catabolic process |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name26S proteasome regulatory subunit RPN2
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP32565
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000173808 | 2-945 | 26S proteasome regulatory subunit RPN2 | |||
Sequence: SLTTAAPLLALLRENQDSVKTYALESINNVVDQLWSEISNELPDIEALYDDDTFSDREMAALIASKVYYNLGEYESAVKYALAAKDRFDIDEKSQFVETIVSKSIEMYVQEASKQYTKDEQFYTKDIIDPKLTSIFERMIEKCLKASELKLALGIALEGYRLDIIESALKSKLDQDSTSENVKIINYLLTLAITTVTNSKFRSSILRKSFDFLMNMPNCDYLTLNKVVVNLNDAGLALQLFKKLKEENDEGLSAQIAFDLVSSASQQLLEILVTELTAQGYDPALLNILSGLPTCDYYNTFLLNNKNIDIGLLNKSKSSLDGKFSLFHTAVSVANGFMHAGTTDNSFIKANLPWLGKAQNWAKFTATASLGVIHKGNLLEGKKVMAPYLPGSRASSRFIKGGSLYGLGLIYAGFGRDTTDYLKNIIVENSGTSGDEDVDVLLHGASLGIGLAAMGSANIEVYEALKEVLYNDSATSGEAAALGMGLCMLGTGKPEAIHDMFTYSQETQHGNITRGLAVGLALINYGRQELADDLITKMLASDESLLRYGGAFTIALAYAGTGNNSAVKRLLHVAVSDSNDDVRRAAVIALGFVLLRDYTTVPRIVQLLSKSHNAHVRCGTAFALGIACAGKGLQSAIDVLDPLTKDPVDFVRQAAMIALSMILIQQTEKLNPQVADINKNFLSVITNKHQEGLAKFGACVAQGIMNAGGRNVTIQLENADTGTLDTKSVVGLVMFSQFWYWFPLAHFLSLSFTPTTVIGIRGSDQAIPKFQMNCYAKEDAFSYPRMYEEASGKEVEKVATAVLSTTARAKARAKKTKKEKGPNEEEKKKEHEEKEKERETNKKGIKETKENDEEFYKNKYSSKPYKVDNMTRILPQQSRYISFIKDDRFVPVRKFKGNNGVVVLRDREPKEPVALIETVRQMKDVNAPLPTPFKVDDNVDFPSA | ||||||
Modified residue | 801 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 932 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
N-acetylated by NAT1.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with UBR1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P32565 | RPN1 P38764 | 4 | EBI-15919, EBI-15913 | |
BINARY | P32565 | RPN13 O13563 | 3 | EBI-15919, EBI-32948 | |
BINARY | P32565 | SEM1 O94742 | 2 | EBI-15919, EBI-31337 | |
BINARY | P32565 | UBR1 P19812 | 2 | EBI-15919, EBI-19909 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 366-399 | PC 1 | ||||
Sequence: TATASLGVIHKGNLLEGKKVMAPYLPGSRASSRF | ||||||
Repeat | 403-440 | PC 2 | ||||
Sequence: GSLYGLGLIYAGFGRDTTDYLKNIIVENSGTSGDEDVD | ||||||
Repeat | 445-479 | PC 3 | ||||
Sequence: GASLGIGLAAMGSANIEVYEALKEVLYNDSATSGE | ||||||
Repeat | 480-514 | PC 4 | ||||
Sequence: AAALGMGLCMLGTGKPEAIHDMFTYSQETQHGNIT | ||||||
Repeat | 516-549 | PC 5 | ||||
Sequence: GLAVGLALINYGRQELADDLITKMLASDESLLRY | ||||||
Repeat | 550-585 | PC 6 | ||||
Sequence: GGAFTIALAYAGTGNNSAVKRLLHVAVSDSNDDVRR | ||||||
Repeat | 586-618 | PC 7 | ||||
Sequence: AAVIALGFVLLRDYTTVPRIVQLLSKSHNAHVR | ||||||
Repeat | 620-654 | PC 8 | ||||
Sequence: GTAFALGIACAGKGLQSAIDVLDPLTKDPVDFVRQ | ||||||
Repeat | 655-692 | PC 9 | ||||
Sequence: AAMIALSMILIQQTEKLNPQVADINKNFLSVITNKHQE | ||||||
Repeat | 698-734 | PC 10 | ||||
Sequence: GACVAQGIMNAGGRNVTIQLENADTGTLDTKSVVGLV | ||||||
Region | 810-851 | Disordered | ||||
Sequence: AKARAKKTKKEKGPNEEEKKKEHEEKEKERETNKKGIKETKE | ||||||
Compositional bias | 818-851 | Basic and acidic residues | ||||
Sequence: KKEKGPNEEEKKKEHEEKEKERETNKKGIKETKE |
Sequence similarities
Belongs to the proteasome subunit S1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length945
- Mass (Da)104,232
- Last updated2007-01-23 v4
- Checksum881E78EBC6BD934F
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 333-334 | in Ref. 1; AAA87613 | ||||
Sequence: SV → RL | ||||||
Compositional bias | 818-851 | Basic and acidic residues | ||||
Sequence: KKEKGPNEEEKKKEHEEKEKERETNKKGIKETKE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L06321 EMBL· GenBank· DDBJ | AAA87613.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z37997 EMBL· GenBank· DDBJ | CAA86095.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006942 EMBL· GenBank· DDBJ | DAA08475.1 EMBL· GenBank· DDBJ | Genomic DNA |